Analysis of the code relating sequence to conformation in proteins: Possible implications for the mechanism of formation of helical regions

摘要: Abstract Information contained in a primary sequence concerned with the helical configuration of folded protein has previously been shown to be associated single residues and pairwise residue combinations. An attempt is made here obtain quantitative estimate these two types information evaluate their separate roles. theory approach used helix-forming from 11 proteins known conformation. The validity measures indicated by precision predictions them. Using alone, observed helices are again predicted but, addition, some non-helical regions also as helical. main effect adding pair delete false helices. It concluded that positive initiate formation and, doing so, call down limited number interactions certain Such code would economical information, leaving many (or higher) combinations dictate tertiary folding. These findings may explained mechanism which residue, expressed energy differences between structure for those residues, dependent presumably on side chain-backbone interactions. From consideration diagrams it suggested loss hydrogen bond COOH-terminal an induced αII conformation, forcing succeeding into lower energy, Occurrence at end region act sharply defined helix-terminating device. suitable points run potentially prevent helix taking place. This keeping earlier observation conformation COOH-termini proteins. relationship folding polypeptides discussed terms micelle hypothesis.