SI2700 Protein Physics 7.5 credits
Proteinfysik
Educational level
Second cycleAcademic level (A-D)
DSubject area
Physics
Grade scale
A, B, C, D, E, FX, F
Course offerings
Spring 13 for programme students
Periods
Spring 13 P3 (7.5 credits)
Application code
60894Start date
2013 week: 2End date
2013 week: 11Language of instruction
EnglishCampus
AlbaNovaNumber of lectures
30 (preliminary)Number of exercises
Tutoring time
DaytimeForm of study
NormalNumber of places
No limitationSchedule
Schedule (new window)Course responsible
Erik Lindahl <erik@kth.se>
Teacher
Erik Lindahl <erik@kth.se>
Part of programme
Spring 14 for programme students
Periods
Spring 14 P3 (7.5 credits)
Application code
60489Start date
2014 week: 4End date
2014 week: 12Language of instruction
EnglishCampus
AlbaNovaNumber of lectures
30 (preliminary)Number of exercises
Tutoring time
DaytimeForm of study
NormalNumber of places
No limitationCourse responsible
Erik Lindahl <erik@kth.se>
Teacher
Erik Lindahl <erik@kth.se>
Part of programme
Spring 14 for programme students
Periods
Spring 14 P3 (7.5 credits)
Application code
60194Start date
2014 week: 4End date
2014 week: 12Language of instruction
EnglishCampus
AlbaNovaNumber of lectures
30 (preliminary)Number of exercises
Tutoring time
DaytimeForm of study
NormalNumber of places
No limitationCourse responsible
Erik Lindahl <erik@kth.se>
Teacher
Erik Lindahl <erik@kth.se>
Learning outcomes
This is an advanced level course in collaboration between Stockholm University and KTH that covers structure, self-organization, and function of the biological macromolecules of life - primarily proteins.
Course main content
Biophysical chemistry: Amino acid conformations & properties, Ramachandran plots. Hydrogen bonds. Thermodynamics, entropy, free energy, and hydrophobic interactions. Electrostatics in biomolecules and solution, disulphide bonds. Properties of polypeptide chains. Alpha, 3-10, and Pi-helices. Parallel and anti-parallel beta sheets. Turns and loops. Conformational changes, helix-coil transitions, stability of secondary structure elements in water and other solvents. Non-polar, polar, and charged amino acid side chains.
Protein structure: Packing of helices and sheets, supersecondary structure. Collagen, keratin, silk, and other simple structures. Structure and function of water-soluble proteins, classification of protein folds. Protein aggregation/misfolding, prions (mad cow disease). Membranes and membrane proteins. Evolution and natural selection of structures.
Protein folding & structure prediction: Anfinsen's Hypothesis. Levinthal's paradox. Kinetics of protein folding. Two-state folding and intermediates. Molten globule or folding nuclei. Energy landscapes. Pathways. Prediction of structure from amino acid sequence. Threading.
Protein function: Docking and binding. Enzyme function. Active sites. Induced fit. Specificity and allostery. Membrane protein function. Protein engineering and design.
Eligibility
Recommended prerequisites: Differential equations, fourier transforms, thermodynamics, electrostatics, numerical methods and programming, elementary quantum mechanics and basic chemistry.
Literature
Finkelstein & Ptitsyn, Protein Physics, Academic Press (2002). ISBN 0-12-256781-1.
Examination
- TEN1 - Examination, 7.5 credits, grade scale: A, B, C, D, E, FX, F
Requirements for final grade
Exam (TEN1; 7,5 university credits).
Offered by
SCI/Theoretical Undergaduate Physics
Examiner
Erik Lindahl <erik@kth.se>
Version
Course plan valid from:
Autumn 07.
Examination information valid from:
Autumn 07.
