Biophysical Chemistry
Biofysikalisk kemi

KFKN10F, 7.5 högskolepoäng

Gäller från och med: Autumn 2017
Beslutad av: Margareta Sandahl
Datum för fastställande: 2017-05-15

Allmänna uppgifter

Avdelning: Biophysical Chemistry
Kurstyp: Gemensam kurs, avancerad nivå och forskarnivå
Kursen ges även på avancerad nivå med kurskod: KFKN10
Undervisningsspråk: English

Syfte

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

Mål

Kunskap och förståelse

För godkänd kurs skall doktoranden

• describe the principal physico-chemical properties of proteins, such as structure, stability, interactions and dynamics
• account for these properties in terms of molecular-level theroetical models
• interpret experimental results from physico-chemical studies of proteins

Färdighet och förmåga

För godkänd kurs skall doktoranden

• use physico-chemical concepts and models to solve problems involving proteins
• apply his/her theoretical knowledge to biotechnological and biomedical problems
• use electronic protein databases
• carry out spectroscopic measurements on proteins

Värderingsförmåga och förhållningssätt

För godkänd kurs skall doktoranden

• read and critically assess the research literature in protein science
• communicate effectively with researchers in protein science

Kursinnehåll

- 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.

Kurslitteratur

The course literature consists of the compendium "Biophysical Chemistry", authored and updated each year by the course teachers, and of manuals for the practicals. For those who want go deeper, the compendium provides a list of selected references and links to the literature.

Kursens undervisningsformer

Undervisningsformer: Föreläsningar, seminarier, laborationer, projekt, studiebesök

Kursens examination

Examinationsformer: Skriftlig tentamen, seminarieföredrag av deltagarna
Betygsskala: Underkänd, godkänd
Examinator:

Antagningsuppgifter

Förutsatta förkunskaper: Under graduate courses in physical chemistry or physics including thermodynamics, intermolecular interactions and molecular dynamics.

Kurstillfällesinformation

Kontaktinformation och övrigt

Kursansvarig: Kristofer Modig <kristofer.modig@lth.lu.se>
Hemsida: http://www.cmps.lu.se/bpc/education/kfk032/