Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-2-22
pubmed:abstractText
Surfactants, which provide a hydrophobic environment, may induce an ordered conformation in polypeptides and proteins that contain a sequence with helix-or beta-forming potential. This hypothesis has been illustrated in circular dichroic studies of oligopeptides and short polypeptides. These peptide-surfactant complexes can form (1) a helix, (2) a beta-form, (3) either form (depending on experimental conditions), or can remain in (4) an ordered form. The induced helix is stable in a surfactant solution below or above its critical micellar concentration, whereas the induced beta-form is usually converted back to an unordered form when the surfactant used is above its critical micellar concentration, or it is transformed into a helix in excess surfactant solution if the peptide has both the helix- and beta-forming potential. In most cases the observed conformations agree with those predicted from the amino acid sequences of the peptides. The induced conformation of a peptide can be destabilized by charges on the side groups having the same sign as that of surfactant ions. Disulfide bonds can inhibit the formation of induced conformation because of steric hindrance. The terminal effect can prevent a peptide from forming an ordered conformation near the NH2- and COOH-terminus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Sequence-dependent conformations of short polypeptides in a hydrophobic environment.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.