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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1989-10-23
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pubmed:abstractText |
A 25-residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made. The peptide contains a helix, beginning as an alpha-helix and ending as a 3(10)-helix, that extends from residue 12 to 23. Several positively charged and polar residues located on this helix are likely to be involved in interactions with DNA. Residues 1-10 appear to adopt a hairpin-like structure.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-64
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2506074-Amides,
pubmed-meshheading:2506074-Animals,
pubmed-meshheading:2506074-Binding Sites,
pubmed-meshheading:2506074-DNA-Binding Proteins,
pubmed-meshheading:2506074-Magnetic Resonance Spectroscopy,
pubmed-meshheading:2506074-Metalloproteins,
pubmed-meshheading:2506074-Molecular Structure,
pubmed-meshheading:2506074-Peptides,
pubmed-meshheading:2506074-Protein Conformation,
pubmed-meshheading:2506074-Xenopus,
pubmed-meshheading:2506074-Zinc
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pubmed:year |
1989
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pubmed:articleTitle |
Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure.
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pubmed:affiliation |
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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