Haixu Tang School of Inforamtics

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Presentation transcript:

Haixu Tang School of Inforamtics Protein structures Haixu Tang School of Inforamtics

A covalent peptide bond

Protein conformation is specified by tts Amino Acid sequence Steric interactions Weak non-covalent bonds hydrogen bonds ionic bonds van der Waals attractions Hydrophobic interaction distribution of its polar and nonpolar amino acids

Protein folding: lowest energy conformation

Protein denaturalization

Visualizing protein conformations Protein structures in atomic level Protein Data Bank (PDB) http://www.rcsb.org Pymol: http://pymol.sourceforge.net/ Rasmol: http://www.umass.edu/microbio/rasmol/

Protein secondary structure

Secondary structure prediction Prefer a-helix: Ala, Leu, Met, Phe, Glu, Gln, His, Lys, Arg (sidechains cover and protect the backbone H-bonds) Prefer b-sheet: Tyr, Trp, Phe, Ile, Val, Thr, Cys (large bulky sidechains) Disrupt secondary structure: Gly, Pro, Ser, Asp, Asn (small, restrained, or sidechain hydrogen bonds)

Coiled coil

Protein Domains Independent structural unit Independent function Independent folding Independent evolve

Protein families

Class Folds Super-families Families Protein structural classification (SCOP: http://scop.mrc-lmb.cam.ac.uk/scop/) Class Folds Super-families Families

Sulfur-sulfur (disulfur) bonds

Assembly of Large Structures

Experimental determination of protein structures X-ray crystallography NMR (Nuclear Magnetic Resonance) Spectroscopy

X-ray crystallography

NMR spectrum