One of the dilemmas in predicting the secondary structure of proteins
from their amino acid propensity for a given conformation is the prese
nce of all amino acids in all types of secondary structure, regardless
of their propensity for that specific structure. One explanation is t
he nucleation hypothesis that only a few residues with a strong propen
sity for the secondary structure, such as the alpha-helix structure, i
nitiates its formation and propagates the structure through indifferen
t sequences until strong breakers terminate the growth on both ends. E
ight 15-mer peptides were studied to examine the alpha-helix nucleatio
n hypothesis. The nucleation sequence of VAEAK, with high helix propen
sity, was mixed with an indifferent sequence of TSDSR in all possible
permutations. From the percent alpha-helix structure derived from the
CD at 222 nm, it appears that helicity does not propagate through the
indifferent sequence. (C) 1994 John Wiley & Sons, Inc.