Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6396
|
pubmed:dateCreated |
1992-11-10
|
pubmed:abstractText |
Short alanine peptides, containing 16 or 17 residues, appear to form alpha-helices in aqueous solution. But the main spectroscopic analyses used on helical peptides (circular dichroism and nuclear magnetic resonance) cannot distinguish between an alpha-helix (in which the ith residue is hydrogen-bonded to residue i + 4; ref. 9) and the next most common peptide helix, the 3(10)-helix10 (i-->i + 3 hydrogen-bonding). To address this problem we have designed single and doubly spin-labelled analogues of alanine-based peptides in which the nitroxide spin label forms an unbranched side chain extending from the sulphur atom of a cysteine residue. Here we report the circular dichroism, Fourier-transform infrared and electron-spin resonance spectra of these peptides under helix-forming conditions. The infrared absorbance gives an amide I' band with a frequency that is substantially different from that observed for alpha-helices. The electron-spin resonance spectra of doubly labelled helices show that the ranking of distances between side chains, around a single turn (residues 4-8), is inconsistent with an alpha-helical structure. Our experiments suggest that the more likely peptide geometry is a 3(10)-helix.
|
pubmed:commentsCorrections | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0028-0836
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
359
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
653-5
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1328890-Alanine,
pubmed-meshheading:1328890-Amino Acid Sequence,
pubmed-meshheading:1328890-Circular Dichroism,
pubmed-meshheading:1328890-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:1328890-Fourier Analysis,
pubmed-meshheading:1328890-Molecular Sequence Data,
pubmed-meshheading:1328890-Peptides,
pubmed-meshheading:1328890-Protein Structure, Secondary,
pubmed-meshheading:1328890-Spectrophotometry, Infrared,
pubmed-meshheading:1328890-Spin Labels
|
pubmed:year |
1992
|
pubmed:articleTitle |
Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution.
|
pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|