Folding of polypeptide chains in proteins: a proposed mechanism for folding.
A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, alpha-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming beta-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in beta-bends, and it is possible to predict the regions of a chain in which a beta-bend will occur with a high degree of reliability.
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000032:analysis; D002417:Cattle; D002645:Chickens; D002918:Chymotrypsin / Q000032:analysis; D003580:Cytochromes / Q000032:analysis; D006736:Horses; D008961:Models, Structural; D009113:Muramidase / Q000032:analysis; D011487:Protein Conformation; D012260:Ribonucleases / Q000032:analysis
D003580:Cytochromes; D012260:Ribonucleases; D009113:Muramidase; D002268:Carboxypeptidases; D002918:Chymotrypsin