Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-9-30
pubmed:abstractText
The effect of sodium dodecyl sulfate (SDS) on the conformation of acetylcholine receptor alpha-subunit synthetic peptides was investigated by circular dichroism. In the presence of SDS (0.01-0.02%), the affinity of a 173-204 32 residue peptide and a 172-227 56 residue peptide for the competitive antagonist alpha-bungarotoxin increases about 10-fold to the nanomolar range. Circular dichroism spectroscopy of these peptides revealed significant changes in the secondary structure of the peptides in the presence of SDS at concentrations below the critical micelle concentration. It is concluded that SDS induces a conformation of the peptides that is conductive to high affinity binding. Carbamylcholine, an acetylcholine analog, produced small but significant changes in the spectrum of the 173-204 peptide. This change could be the result of agonist-induced conformational changes in this region of the acetylcholine receptor alpha-subunit or to changes in the asymmetric environments of aromatic chromophores in the binding site. These studies demonstrate that synthetic peptides alone are capable of retaining significant functional activity and contain significant secondary structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0169-328X
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Sodium dodecyl sulfate- and carbamylcholine-induced changes in circular dichroism spectra of acetylcholine receptor synthetic peptides.
pubmed:affiliation
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.