Premium
A CD study of the α‐helix nucleation hypothesis
Author(s) -
Toumadje Arazdordi,
Johnson W. Curtis
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360340715
Subject(s) - chemistry , nucleation , helix (gastropod) , computational biology , zoology , organic chemistry , biology , gastropoda
One of the dilemmas in predicting the secondary structure of proteins from their amino acid propensity for a given conformation is the presence of all amino acids in all types of secondary structure, regardless of their propensity for that specific structure. One explanation is the nucleation hypothesis that only a few residues with a strong propensity for the secondary structure, such as the α‐helix structure, initiates its formation and propagates the structure through indifferent sequences until strong breakers terminate the growth on both ends. Eight 15‐mer peptides were studied to examine the α‐helix nucleation hypothesis. The nucleation sequence of VAEAK, with high helix propensity, was mixed with an indifferent sequence of TSDSR in all possible permutations. From the percent α‐helix structure derived from the CD at 222 nm, it appears that helicity does not propagate through the indifferent sequence. © 1994 John Wiley & Sons, Inc.