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