BCH 2333 Lecture 9: Lecture 9 - Folding
2 Mar 2017
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Document Summary
Chap 5 section 1-3 will not be on midterm. Usually include some kind of beta turn (the green loop. Basically two antiparallel strands held together with a loop. Very compact structure of 4 beta strands that are antiparallel. Usually a right handed helix (cause they"re more common) Hydrophobic interactions on the alpha helix bond with residues on the beta sheet. Bent h bonding banding (parallel) which makes it less stable than antiparallel beta sheet. 50% of regular secondary structures are helices and beta pleated sheets, the other 50% are coil and loop conformations. Coil = structure, random coil = not structure. Globular proteins consist of largely straight runs of secondary structure joined by stretches of polypeptide that abruptly change directions. Usually connect strands of antiparallel beta-sheets and alpha helices. Almost always occur on the surface of a protein. Mostly hydrophilic because they are on the outside. Involve 4 successive amino acid residues arranged in one of two ways.
