Doctoral student courses
Lund University
Lund University has a range of courses available for the employees, some of which are suitable for PhD students.
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Faculty-wide doctoral student courses
LTH and Faculty of science offers courses for doctoral students. Some of these courses are mandatory.
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The courses given in the Faculty of Science research schools are open for PhD students at the faculty.
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Other departments at LTH and the Faculty of Science have doctoral courses that might suitable for PhD students in Chemistry. Check the respective departments’ webpages.
Department of Chemistry
General Courses
The Department of Chemistry offers a range of general doctoral courses. Some of the courses are mandatory for PhD students at the department. See the information to the right or at the bottom of the page on mobilephone.
The course in brief:
The goal of the course is to enhance the doctoral students' knowledge in literature searching. Participants will be introduced to the coverage, precision and quality of different search engines and learn how to improve their literature searches through a structured customisation of keywords and the use of different search operators. The course also discusses the advantages and disadvantages of different search strategies, tools, and databases.
Course content
The course consists of a series of lectures that cover available databases relevant to chemistry, search strategies, and relevant search terms within chemistry. Additionally, there is a brief project where participants conduct a preliminary search with an associated search strategy within their research field.
The course in brief:
The course is compulsory for all graduate students at KILU and recommanded for other graduate students at KC that have experimental research or teaching. The course should give necessary knowledge to perform laboratory work in a safe manner.
Course content
The course consists of the following: -the environmental work at Chemistry Center and Lund University -hazards concerning chemicals -protection gear -safety regulations -laws and regulations for environmental safety -hazard evaluations -accidents.
The course in brief:
The aim of the course is to supply the student with fundamental theoretical knowledge in experimental design, multivariate statistics and quality assurance, and skills in the use of associated statistical tools. The course also aims to prepare the participants for future needs of planning experiments and dealing with large quantities of data.
Course content
The course covers the basics, principles and limitations for the most common methods for multivariate statistics (analysis of variance, principal component analysis and partial least squares regression), experimental design (super-saturated and factorial designs) and method validation with a focus on practical use. Great emphasis will be placed on covering a wide range of applications of these techniques which will aid in selecting appropriate techniques for specific research questions. The practical elements aim at giving the participants basic knowledge in selecting and applying methods for different applications.
The course in brief:
The aim of the course is to offer recently accepted graduate students at KILU an introduction to the workplace with respect to general employment conditions, key tools for documentation of own work, basic level knowledge of academic code of conduct regarding academic honesty and interpersonal relations.
Course content
The content of the course includes the following topics: goals and obligations of graduate studies, general and individual study plans, code of conduct for academic honesty and interpersonal relations, information regarding graduate course programme, scientific information management and library resources, organization of KILU, introduction to the use of LUBox or similar.
The course in brief:
The aim of the course is to offer recently accepted graduate students at KILU an extended introduction to the work place concerning employment conditions and expected progression of skills. The three areas research, education and outreach activities are discussed in relation to i) the Higher Education Ordinance (1993:100) (HEO), and ii) the concept “Doctorateness”. The areas education and outreach activities are further discussed though an introductory session aiming at highlighting the more important aspects of assistant teaching in laboratory settings. Chemistry-relevant research activities are exemplified through visits at the individual research units at KILU, and here with a focus on activities utilizing common, largescale infrastructure.
Course content
The course includes the following topics: guided visits to the four research centres at KILU with information regarding up-to-date research and infrastructure, popular science inspiration lecture, half-day workshop with focus on pedagogics of particular relevance for teaching and supervision of undergraduate students, half-day workshop on the theme “My graduate education – freedom with responsibility”.
The course in brief:
The course provides the participants with knowledge about how to effectively communicate scientific results using a poster.
Course content
- Introduction to the field of scientific communication
- Obtaining practical knowledge about scientific communication
- Practicing presenting research results in a poster format
- Critically assessment of visual presentation of research results
- Active exchange of knowledge about current research within the research topic/department
The course in brief:
The course provides the participants with knowledge about how effectively present their research in a short and precise “elevator pitch”.
Course content
- Further introduction to the field of scientific communication
- Obtaining practical knowledge about scientific communication
- Practicing presenting an “elevator pitch”
- Critically assessing other “elevator pitches”
- Active exchange of knowledge about current research within the research topic/department
The course in brief:
The course provides the participants with knowledge how to present a clear and engaging research talk (10-15 minutes in length).
Course content
- Further introduction to the field of scientific communication
- Obtaining practical knowledge about scientific communication
- Plan, design and execute a research talk
- Critical review of other research talks
- Active exchange of knowledge about current research within the research topic/department
Subject specific courses
The units/divisions offer a range of specialized courses. Some of these may be mandatory for certain research subject. Check the general syllabus (ASP) for the research subject. Several of the courses run on demand while others run regularly.
The course in brief:
The aim of the course is to give synoptic knowledge of applied mathematics with focus
on advanced problems in natural science and medicine. The course includes advanced
use of mathematical software for research-related practical problem solving.
Course content
The course is focused on advanced mathematical topics related to the research in the
field of natural science. In particular, the course covers linear algebra, partial
differentiation equations, special functions, variations, functions of complex variables,
tensors, numerical methods, probability and statistics
The course in brief
The aim is to provide deep and theoretical knowledge about the physiology, function and exploitation potential of living microbial cells.
Course content
The course will provide the PhD student a profound knowledge on the relationships between microorganisms, their function in nature, their application in industry and their potential for solving environmental problems. The course covers the metabolism and genetics of the cell, microbial diversity, and the use of microbes for industrial production and bioremediation.
The course in brief:
The aim is to provide deep and theoretical knowledge about the structure, physiology, function and possibilities to exploit living microbial cells. With this deeper knowledge of relationships between microorganisms, and their structure and function in nature, the course also provides the PhD student to integrate this knowledge with microbial applications in industry and for solving environmental problems. The course covers the genetics and metabolism of the cell, microbial ecology, and the use of microbes for industrial production and bioremediation.
Course content
Microbiology is an exceptionally broad discipline encompassing specialities as diverse as biochemistry, cell biology, genetics, taxonomy, pathogenic bacteriology, food and industrial microbiology and ecology. The aim of “Advanced Microbiology” is to cover all aspects of microbiology during a series of seminars. The participants are limited to a maximum of four graduate students. Two teachers contribute in the seminars. The course ends with an oral presentation in public.
The course in brief
The aim of the course is for the student to acquire advanced knowledge about Nuclear Magnetic Resonance (NMR) theory and applications in studies of bio-macromolecular structure and dynamics. The course focuses on methods for studying proteins, but the underlying theory is equally applicable to essentially any molecule in the liquid phase.
Course content
The course begins with basic theory on NMR, including an introduction to quantum mechanics, quantum statistical mechanics, the density matrix and product operator formalisms. The course then covers the theory of multi-dimensional spectroscopy, including frequency labeling of coherences, coherence transfer and mixing, and coherence pathway selection. The course also covers experimental techniques and practical aspects, including data acquisition and data processing.
The course in brief:
The course aims to deepen and broaden the students knowledge of modern synthetic methods. The course will broadly cover synthetic methods with respect to their mechanisms and frontier orbital descriptions. Specifically, the course will cover oxidations and reductions, functional group interconversions, carbon-carbon bond forming reactions, fundamental transition metal catalysis, cycloadditions, rearrangements, aromatic chemistry, and vissa applications in multi-step synthesis.
Course content
Lectures are given on broadly selected topics in advanced organic synthesis. A mandatory seminar is associated with each lecture. Assignments for the seminars will be handed out. Individual hand in assignments may replace or compliment seminars. Each student will present a 25 minute in-depth lecture on a topic within the course. Part of the presentation assignment is to give constructive feedback on a peer presentation.
The course in brief:
The aim of the course is to give a deep knowledge and broad understanding of modern organometallic chemistry and its applications in synthesis and catalysis.
Course content
The course covers models for describing bonding and reactivity in organometallic chemistry, typical organometallic ligands and reactions, and the use of organometallic reagents in catalysis and organic synthesis. It also provides examples of industrial applications for organometallic chemistry.
The course in brief:
The course in advanced physical organic chemistry gives a deeper understanding of the physical properties of organic molecules as well as organic reaction mechanisms.
Course content
The material is divided into nine thematic sessions: chemical bond, acids and bases, carbocations, ionic reactions, stereoelectronic effects, the carbonyl group, radical reactions, pericyclic reactions, and photochemistry. A more complex session finishes the course. An individual project concerning physical organic aspects of the research project is also a part of the course. Each session consists of a number of questions which will be presented orally and written.
The course in brief:
The course provides a deep knowledge and understanding about the physical and organic chemistry regarding polymerization reactions and polymeric materials.
Course content
Different polymerization reactions (step-growth, chain and ring-opening polymerizations), their kinetics, thermodynamics and applicability for different polymers and materials. Relationships between kinetics and molecular weight. Complex polymer structures. Copolymerization. Stereo-selective polymerization. Chemical modification (functionalization) of polymers. Industrial processes.
The course in brief:
The course shall give deep knowledge and understanding about different concepts concerning physical properties of polymers, primarily in the solid state.
Course content
Polymers in the amorphous state, the liquid crystalline state and the crystalline state. The glass-rubber transition. Cross-linked polymers and rubber elasticity. Polymer viscoelasticity. Mechanical behavior of polymers. Multicomponent polymeric systems.
The course in brief:
The course aims to provide a deeper understanding of of Statistical Mechanics theories, methods, and tools. The course also aims to bridge the microscopic properties of single particles (Statistical Mechanics) and macroscopic properties (Thermodynamics). A sub-goal is to build an understanding of the link between interactions and dynamics. The students should also get an update on recent advances in the field.
Course content
The course starts with a repetition of basic statistical-mechanical concepts, methods, and tools. It then continues with more advanced theories for liquids and solutions, simulation methods as well as transport properties and dynamics for liquids and
solutions. The course is given in a thematic form with lectures and tutorials (self studies) as well as laboratory work and laboratory report hand-ins which all highlight the different themes.
The course in brief:
The aim of the course is to enable the participants to acquire in-depth physicochemical knowledge in the field of surface and colloid chemistry from a molecular perspective and a quantitative understanding of selected fundamental colloidal and interfacial phenomena.
Course content
The theoretical component contains lectures and tutorials that treat surface and colloid chemistry from a molecular physicochemical perspective. Key themes comprise the self-association of amphiphilic molecules, polymers in colloidal systems, phase equilibria in solutions, interfacial phenomena, and electrostatic interactions between molecules and surfaces with applications in colloidal stability.
The practical component consists of laboratory classes, computer exercises and a literature exercise. The laboratory classes introduce central experimental techniques in surface and colloid chemistry and are designed
to, together with the computer exercises, illustrate central phenomena treated in the theoretical component. The literature exercise includes literature searches in a database, oral presentation of a research article and participation in discussions at the oral presentations.
The course in brief:
The course aims at giving synoptic knowledge of the use of FORTRAN computer language to achieve efficiency in communication with a computational hardware. The course focuses on implementing efficient programming practice.
Course content
The course covers programming aspects in FORTRAN computer language, which are related to software design and hardware architecture. Specific topics covered in the course includes: IEEE standards for machine representation of data, accuracy of the arithmetic calculations, stability of numerical algorithms, most common problems with code optimization, efficient use of computer memory.
The course in brief:
The course aims to provide advanced theoretical insight into commonly occurring modern separation techniques, such as chromatography, mass spectrometry and capillary electrophoresis.
The course also aims to develop the students’ ability to independently select and optimise appropriate separation techniques/methods and to provide a coherent overview of the subject.
Course content
Lectures: Advanced theoretical treatment of chromatographic separation and the underlying distribution and adsorption equilibria. Instrumentation and experimental technology for modern liquid chromatography and gas chromatography. Coupling gas chromatography and liquid chromatography to mass spectrometry. Basic orientation on capillary electrophoresis.
Laboratory work: Experimental technology for high resolution liquid chromatography and massspectrometry. Optimisation of HPLC systems with different combinations of mobile and stationary phases. Gas chromatography with capillary columns, injection techniques and the use of mass spectrometric detection.
Literature project: Chiral separations with oral and written presentation.
The course in brief:
The aim of the course is to provide in-depth theoretical and practical knowledge in sampling, sample preparation, quality assurance, chromatography, mass spectrometry, detection techniques and classical analytical chemistry techniques. The course further aims to develop the doctoral student's ability to independently read, compile and orally present theory in a specific area.
Course content
The course is divided into six different parts: i) Classical analytical chemistry (corresp. to 2 hp); ii) Quality assurance (corresp. to 2 hp); iii) Sampling and sample preparation (corresp. to 3 hp); iv) Chromatography (corresp. to 3 hp); v) Mass spectrometry (corresp. to 3 hp); and vi) Detection techniques (corresp. to 2 hp). Each part contains compulsory literature and instructions on specific learning outcomes. In addition to compulsory literature, participants are expected to search for and read literature on their own where the compulsory is not sufficient.
The course in brief:
This course develops the basic skills for applied scientific data treatment with a focus on the chemical and physical sciences. The course contains theoretical as well as applied parts to enable the students to perform data analysis in their respective subject with a widely used and freely available computing language (Python).
Course content:
The course is focused on the practical skills necessary to analyze data in chemical sciences. Each topic will be introduced with a short theoretical background followed by a practical tutorial introducing the key concepts and methods on tutorial data and finally on the student’s own dataset. The course deals with the following concepts:
- Introduction to Python and data handling.
- Importing, cleaning, and plotting data.
- Statistical description and evaluation of data and data correlations.
- Creation of advanced graphs in publication quality.
- Creation of simple functions e.g. cost functions for optimization tasks.
- Introduction to singular component analysis (SVD, PCA), model formulations, and optimization routines.
- Introduction to image handling and manipulation using self-defined and pre-defined libraries.
- Introduction to artificial intelligence for categorization of image information.
- Introduction to communication with instruments.
The course in brief:
The course content
Lectures: Advanced theoretical treatment of liquid chromatographic separation and the underlying distribution and adsorption equilibria. Instrumentation and experimental technology for high-performance liquid chromatography and universal and selective detectors. Coupling high-performance liquid chromatography to high resolution mass spectrometry. Sample preparation of biological samples prior to liquid chromatographic analysis.
Laboratory work: Experimental technology for high-performance liquid chromatography. Optimisation of HPLC systems with different combinations of mobile phases for quantitative and qualitative analysis of small molecules. Demonstration of high-performance liquid chromatography in combination with high-resolution mass spectrometry for qualitative analysis of small molecules.
The course in brief:
The course aims at giving the student: - molecular-level understanding of the structure, stability, interactions and dynamics of proteins - knowledge about the principal physical methods used in modern protein science - practical experience in using some of these methods - the knowledge base needed to use and critically assess the protein research literature.
Course contents
The chemical building-blocks and three-dimensional structures of proteins: Structure analysis by X-ray crystallography; Structure and sequence databases; Bioinformatics. - Protein characterization by optical spectroscopy: Physical principles and applications of fluorescence and circular dichroism spectroscopy. - Polypeptide conformation: Models of polymer conformation and conformational transitions; Conformational entropy; Folding cooperativity. - Protein energetics and stability: Packing; Hydration; Electrostatics; Thermal and solvent-induced denaturation; Differential scanning calorimetry. - Protein dynamics: Kinetic models; Proton exchange; Diffusion control; Protein folding; Computer simulation of proteins. - Nuclear magnetic resonance: Principles of NMR spectroscopy and relaxation; Analysis of structure, interactions and dynamics of proteins in solution. - Association processes: Ligand binding; Allostery; Protein aggregation; Isothermal titration calorimetry; Surface plasmon resonance.
The course in brief:
Deepened knowledge on the biophysical chemistry of proteins with emphasis on properties rather than methods.
Upon completion of the course, the student shall be able to:
- Describe the structures and functions of several protein families
- Describe physical properties of proteins including surface properties and hydrodynamics
- Define the molecular driving forces that govern the, structure, folding and stability of proteins
- Demonstrate acquaintance with the literature in the area, including classical as well as recent papers
- Calculate accessible surface area and other properties for proteins with known structure
- Analyse ligand binding and protein stabilitet
- Use the literature and databases to improve the scientific level of protein research projects.
- Explain protein properties and phenomena from a physicochemical perspective
- Discuss and evaluate both fundamental texts and advanced applications in the area.
- Summarize the knowledge level in classical as well as modern literature in the area.
Course content
The course is set up around the following topics:
- Protein sequences
- Protein targeting and modification
- Protein structure taxonomy
- Structure of Folded proteins
- Protein stability
- Extremophiles
- Hydrodynamic properties
- Protein folding and aggregation
- Ligand Binding
- The relation between sequence and structure
- Protein dynamics
- Membrane proteins
- Evolution
The course in brief:
Course content
Reaction rates, rate laws, reversible and consecutive reactions, steady state approximation, deduction of reaction mechanisms, transition-state theory, chain reactions, activation parameters, experimental methods, dynamic NMR
The course in brief:
Course content
The course deals with coordination chemistry and organometallic chemistry. In this area, structure and bonding theory, reaction mechanisms and characterization methods (NMR and molecular spectroscopy) are studied. The course also covers organometallic type reactions, use of organometallic reagents in catalysis and organic synthesis, and chemical databases. The role of metals in biological systems is also addressed.
For more information about the course Coordination and organometallic chemistry - NKE012F, please visit the course information website on Canvas.
The course in brief:
The aim of the course is to give participants practical experience and theoretical knowledge of PCR-based analysis of nucleic acids (RNA/DNA) through lectures, wet laboratory work and discussions.
Course content
The course consists of compulsory lectures, seminars, workshops, literature assignments and wet labs that are performed individually or in groups of 2-3 people.
The course in brief:
The course aims at giving synoptic knowledge of applied mathematics with focus on problems in natural science, in particular in physical chemistry. The course also aims at introducing the use of mathematical software.
Course content
The course covers the basic chapters in advance mathematics and their applications to chemistry. The particular topics includes preliminary calculus, complex numbers, series and limits, vectors and matrices, partial differentiation and multiple integrals, vector calculus and differentiation equations.
For more information about the course Essential mathematical tools for chemists - NKE010F, please visit the course information website on Canvas.
The course in brief:
The aim of the course is to supply the student with fundamental theoretical knowledge in experimental design, multivariate statistics and quality assurance, and skills in the use of associated statistical tools. The course also aims to prepare the participants for future needs of planning experiments and dealing with large quantities of data.
Course content:
The course covers the basics, principles and limitations for the most common methods for multivariate statistics (analysis of variance, principal component analysis and partial least squares regression), experimental design (super-saturated and factorial designs) and method validation with a focus on practical use. Great emphasis will be placed on covering a wide range of applications of these techniques which will aid in selecting appropriate techniques for specific research questions. The practical elements aim at giving the participants basic knowledge in selecting and applying methods for different applications.
The course in brief:
The course aims to provide a deeper understanding of some of the most important experimental methods used to determine the three-dimensional structures of proteins, as a basis for understanding their biological functions. We also aim at an understanding of the forces that underpin the three-dimensional structure of proteins, as well as a basic understanding of the methods used in structure-based drug design.
Course content
Lectures:
Basic knowledge of protein structure: polypeptide conformation. Protein secondary and three- dimensional structure. Stability, dynamics and interactions of proteins: packing and electrostatics. Principles of X-ray crystallography, neutron crystallography, small angle X-ray and neutron scattering. Ligand binding and structure-based drug design.
Laboratory work and computer exercises:
Training in the relevant theoretical and experimental methods described for the study of protein structure and dynamics. Includes protein crystallization, data collection at MAX IV, data processing, structure determination and modelling, as well as a simple exercise in ligand docking.
For more information about the course Experimental Structural Biology - NAKE011, please visit the course information website on Canvas.
The course in brief:
The course aims to deepen and broaden the students knowledge of modern organic synthesis strategies and methods. The course will cover methods with respect to synthesis planning, retrosynthetic analysis, and the synthon approach with respect to functional group strategies and stereochemical strategies, as well as target structure and topology.
Course content
Seminars on selected topics in advanced contemporary organic synthesis planning and retro-synthetic analysis. Each student will present an in-depth seminar on a topic within the course. Topics will be selected by the student with advise from course teachers. Part of the presentation assignment is feedback from peers and teachers.
The course in brief:
Course content
Physical and chemical properties of aromatic(main part) and non-aromatic heterocyclic compounds. The synthesis of the ring systems of aromatic (main part) and non-aromatic heterocyclic compounds. The derivatization of the ring systems of aromatic (main part) and non-aromatic heterocyclic compounds. The mechanisms for the formation and derivatization of the different ring systems of heterocyclic compounds. Although the course course comprises both aromatic and non-aromatic heterocyclic compounds, the emphasis is on aromatic systems.
The course in brief:
The aim of the course is for the student to learn basic knowledge about Nuclear Magnetic Resonance (NMR) and its applications in the studies of structure and dynamics in macromolecular and colloidal systems. The course also addresses imaging techniques and methods for the studies of solid materials.
Course content
Lectures: The course begins with basic theory for Nuclear Magnetic Resonance, including an introduction to quantum mechanics. Then follow lectures on chemical shift, nuclear spin interactions, spin dynamics, chemical exchange, relaxation, multi-dimensional applications (including structure determination of macromolecules) and methods for imaging and the study of self-diffusion. The last part of the course is a possibility for each student to make a deeper descent into a subject that he or she finds interesting and relevant. A visit to the MR department at the Lund University Hospital might be offered. Practicals: An introduction to the data treatment in NMR (including topics like the Fourier transform and artefacts) is followed by practicals covering chemical exchange, relaxation, imaging and self diffusion. An extra practical might be offered as a part of the student’s intensifying task. That practical might cover, for example, structure determination, solid state NMR or molecular dynamics.
The course in brief:
The aim of the course is to give deep knowledge in and broad understanding of medicinal chemistry and pharmacological principles from a molecular perspective.
Course content
The course discusses the most common target molecules for drug development, general pharmacodynamic/pharmacokinetic principles and strategies for drug discovery and development. It integrates organic, physical, theoretical and biochemistry to describe how a given drug molecule can interact with disease-relevant target molecules, as well as how drug molecules can be chemically optimised with respect to pharmacodynamic and pharmacokinetic properties. Relationships between chemical structure and biological activity are central in the teaching content. This is exemplified in the course with antivirals, antibiotics, cancer drugs, PNS/CNS drugs (adrenergic, cholinergic, and opiate receptors) and ulcer drugs. Biologicals are describes, discussed,an d compared with small organic molecules from a drug perspective.
The course in brief:
The purpose of the course is to provide participants with practical experience and theoretical knowledge of flow cytometric analysis of microbial cell populations.
Course content
The course consists of compulsory lectures, seminars, workshops, oral or written exercises, and experimental projects carried out in groups of 1-4 people.
The course in brief:
The course aims to provide good knowledge of the basic theories about chemical bonds and intermolecular interaction and how they control the behaviour of matter.
Course content
Lectures: The course covers two areas, quantum mechanics and quantum chemistry. The quantum mechanics section takes up the basic equations that control the behaviour of microscopic particles. The quantum chemical section takes up how these basic equations control the behaviour of atoms and molecules.
Project: A small project will be carried out, with focus on quantum chemistry.
The course in brief:
The aim of the course is for the student to acquire advanced knowledge about NMR relaxation theory and applications in studies of bio-macromolecular structure and dynamics. The course focuses on methods for studying proteins, but the underlying theory is equally applicable to essentially any molecule in the liquid phase.
Course content
The course begins with basic theory on NMR relaxation, including the random-phase model for transverse relaxation, Bloch-Wangsness-Redfield theory, stochastic processes, correlation functions and spectral density functions, relaxation mechanisms, interference effects, and chemical exchange effects. The course then covers the experimental approaches to study molecular dynamics using NMR relaxation.
The course in brief:
The course aims to train new or early users to design, plan, prepare, perform, and analyse an x-ray absorption spectroscopy experiment at a synchrotron beamline or at a table-top XAS machine.
Course content
The course contains three major elements:
1. Lectures/seminars with focus on:
- Creation, interaction and measurement with/of X-rays
- Concept, design and analysis of XAS measurements
- Large-scale facilities, proposal and publication of scientific results
2. Practical data analysis
- EXAFS analysis of molecular and solid samples
- XANES analysis of molecular, solid and nanoparticulate samples
- Linear combination analysis in XANES/EXAFS of diverse mixed samples (e.g. earth, ash) or different metal alloys and crystalline materials (e.g. CZTS)
3. Practical work including sample preparations, safety training, MAX IV tour and measurements.
The course in brief:
The course aims to introduce participants to fragment-based lead discovery, which is an approach to discover small molecule compounds binding a target protein of medical interest and then further use that information to develop potential therapeutic compounds. The process includes biophysical techniques as well as structural biology methods such as X-ray
crystallography and computational chemistry. Participants will learn the theory of the whole process of fragment-based lead development, will be introduced to available relevant national and international infrastructures and will learn about sample preparation and data collection. Furthermore, the participants will work individually with structural models and learn about X-ray data processing and analysis.
Course content:
The course consists of lectures, practical exercises and workshops, individual work and preparation of a presentation.
Part 1:
- Symposium with invited speakers presenting current research in the field.
- Lectures covering relevant topics in the field:
- Biophysical methods (WAC [weak affinity chromatography], NMR, SPR).
- Strategies in medicinal chemistry and SAR studies
- Principles of ADMET analysis
- Necessary infrastructure
- Lectures on how X-ray crystallography is used in fragment screening and introduction to other structural methods relevant for drug discovery (serial crystallography, neutron crystallography and cryo-EM).
Part 2:
- Visit to MAX IV with demonstration of protein crystal handling, X-ray data acquisition and analysis.
- Workshop on structural models and computational chemistry methods for fragment analysis and development.
The course in brief:
Course content
The course gives an introduction in how to use protein mass spectrometry as a tool in protein science. Practical parts including protein and peptide sample preparations, deposition with different techniques and the use of chromatographic separations for complex samples prior to mass spectrometry analysis. Manual and automated mass spectrometry acquisition of intact protein and peptide mass determination and determination of peptide sequence information. Basic data handling of mass spectrometry data for protein identification, assessment of PTMs and determination of amino acid sequences.
The course in brief:
Optical techniques are used to obtain information about the structure, interactions, and dynamics of proteins. It is, therefore, the aim of the course to provide the necessary knowledge to collect “good and reliable” data, to understand preprocessing routines, and eventually to analyze the data.
Course content
The course consists of compulsory lectures, tutorials, lab practicals, and presentations. The week of study is articulated as follows: - Short description of the techniques and what they can do - Short description of advanced usages of the techniques and analysis (accessories and software) - Short description and tutorial on data analysis, especially secondary structure estimation and conformational transitions - Lab practicals with all four techniques on standard proteins and students' proteins (data collection and analysis).
The course in brief:
The course aims to provide the knowledge of the modern theories and techniques used in quantum chemistry of molecules, extended systems and solutions.
After completing the course students have the following skills and knowledge:
1. have an understanding of state-of-the-art theories in the field of quantum chemistry
2. know how to design and perform research using quantum chemical programs
3. be able to critically analyze of the results obtained by different computational approaches
Course content
The lectures cover the main modern methods in the field of quantum chemistry, including Hartree-Fock theory, Density Functional Theory, multiconfigurational methods. A special attention is paid to the description of extended systems, including force fields and the QM/MM technique.
The course is followed by an individual research project focused on applicability of different computational methods used for description of the ground and excited states of various molecules.
The course in brief:
Learning outcomes
On completion of the course, participants shall be able to:
• Account for basic knowledge and understanding of different scattering methods and how they can be used to study structure and dynamics of colloidal dispersions.
• Describe the general experimental setups for light scattering and small angle scattering of X-rays and neutrons.
• Calculate, analyze and interpret the results from static scattering experiments from colloidal dispersions in terms of the static structure factor and various form factors and the results from dynamic light scattering experiments from colloidal dispersions.
• Compute the static scattering from a dispersion of spherical colloidal particles. Judgement and approach
• Explain the general principles of dynamic light scattering experiments, and what
information that may be obtained from such experiments.
Course content
Lectures on basic scattering theory and a derivation, from basic principles, of the scattering from a dispersion of spherical colloidal particles. This is followed by a presentation of different experimental methods, such as small angle neutron scattering (SANS), small angle X-ray scattering (SAXS), and static and dynamic light scattering. As the main model system, we treat dispersions of spherical particles but non-spherical particles will also be discussed.
The course in brief:
On completion of the course, participants shall be able to:
• Account for principles of mass spectrometry, including fundamental design of the more common instruments and how these function.
• Account for the most common mass spectrometry applications, including possibilities and limitations for analysis of small molecules.
• Describe the impact of isotope distributions, charge states and fragmentation on the appearance of the mass spectrum, and be able to show how this information can be used to identify small molecules.
• Analyze and interpret data derived by mass spectrometry.
• Design a method for analysis of small molecules.
• Perform simple chromatographic separations and mass spectrometric analyses of small molecules.
• Describe what type of results that may be obtained from mass spectrometric analyses.
• Compare results from different analyses and be able to understand and explain differences and similarities between them.
• Compile results from a mass spectrometric analysis in a report and a presentation.
Course content
The course covers the most common ionization techniques (electron ionization, chemical ionization, electrospray ionization, atmospheric pressure chemical and photo ionization) and mass analyzers (quadrupole, ion trap, time-of-flight, orbitrap, and combinations of these). The function of these will be connected to their applicability in various fields of applications. Different ways of using the mass spectrometer (scan, single ion monitoring, single and multiple reaction monitoring, targeted and data dependent tandem mass spectrometry) will be discussed. The relation between molecular structure, isotope composition, adduct formation and fragmentation, and the use of this information for identification purposes will be covered. The practical modules aim at giving the students fundamental knowledge in writing methods and using mass spectrometers.
The course in brief:
The course aims to provide a basic understanding of Statistical Mechanics. An important goal is to provide a deeper understanding of Entropy, thus bridging the apparent contradiction between a microscopic (Statistical Mechanics) and a macroscopic (Thermodynamics) treatment.
Course content:
Lectures: The course starts with an introduction of basic Statistical Mechanical concepts. Thermodynamical transformations are compared with corresponding Statistical Mechanical ensembles. Approximate theories for liquids and solutions. Simulation methods.
Tutorials: Here, the student acquires skills to utilize Statistical Mechanical tools.
Lectures and tutorials correspond to 6 credits (NAKE010).
Laboratory work and hand-ins correspond to 1.5 hp. (Cannot be accredited separate from
the lecture part)
The course in brief:
The course aims to provide a basic understanding of Statistical Mechanics. An important goal is to provide a deeper understanding of Entropy, thus bridging the apparent contradiction between a microscopic (Statistical Mechanics) and a macroscopic (Thermodynamics) treatment.
Course content:
Lectures: The course starts with an introduction of basic Statistical Mechanical concepts. Thermodynamical transformations are compared with corresponding Statistical Mechanical ensembles. Approximate theories for liquids and solutions. Simulation methods.
Tutorials: Here, the student acquires skills to utilize Statistical Mechanical tools.
Lectures and tutorials correspond to 6 credits (NAKE010).
The course in brief:
On completion of the course, the student should be able to:
• Interpret simple phase diagrams and judge their implication in the design of a supercritical fluid process
• Describe different application areas of supercritical fluid technology
• Summarize the state of the art research and industry processes in supercritical fluid technology
• Critically discuss different strategies in supercritical fluid processing, the equipment involved, and safety aspects
• Discuss the role of supercritical fluid technology in sustainable development
Course content:
Lectures: (i) solubility of small molecules in supercritical fluids; (ii) interpretation of phase diagrams; (iii) equipment and safety; and (iv) fundamentals and applications of supercritical fluid extraction, chromatography, polymer processing, particle formation, reactions and biocatalysis.
Laboratory work: three half-days of lab work: (i) supercritical fluid extraction; (ii) supercritical fluid chromatography; and (iii) particle formation.
Invited lectures: invited lecture(s) in selected field(s) of supercritical fluid technology.
Doctoral student KILU/LTH
Mandatory courses
At KILU
- KILU Introduction 1 – NKE007F – 1 credit
- Environmental issues and hazards in the chemical research laboratory - KAS001F – 2 credits
At LTH
- Introductory Course for Newly Admitted doctoral Students - GEM056F – 2 credits
- Research Ethics - GEM090F – 3 credits
In addition, for PhD students who are teaching:
- Introduction to Teaching and Learning in Higher Education - GEM002F – 5 credits
Doctoral student KILU/Faculty of Science
Mandatory courses
At KILU
- KILU Introduction 1 – NKE007F – 1 credit
- Environmental issues and hazards in the chemical research laboratory - KAS001F – 2 credits
At the Faculty of Science
- Introduction course for PhD students at the Faculty of Science - 0,5 credits
- Research Ethics - NMN001F – 3 credits
In addition, for PhD students who are teaching:
- Teaching and Learning in Higher Education – Theory and Practice - NMN002F - 3 credits