Ontology highlight
ABSTRACT:
SUBMITTER: He MM
PROVIDER: S-EPMC2286564 | biostudies-literature | 2004 Oct
REPOSITORIES: biostudies-literature
He Molly M MM Wood Zachary A ZA Baase Walter A WA Xiao Hong H Matthews Brian W BW
Protein science : a publication of the Protein Society 20040831 10
In general, alpha-helical conformations in proteins depend in large part on the amino acid residues within the helix and their proximal interactions. For example, an alanine residue has a high propensity to adopt an alpha-helical conformation, whereas that of a glycine residue is low. The sequence preferences for beta-sheet formation are less obvious. To identify the factors that influence beta-sheet conformation, a series of scanning polyalanine mutations were made within the strands and associ ...[more]