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pubmed-article:3144279pubmed:abstractTextThe structure of a peptide from the transforming region (residues 4-20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp12 containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.lld:pubmed
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pubmed-article:3144279pubmed:authorpubmed-author:ChenJJlld:pubmed
pubmed-article:3144279pubmed:authorpubmed-author:MARSP HPHlld:pubmed
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pubmed-article:3144279pubmed:pagination776-82lld:pubmed
pubmed-article:3144279pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:3144279pubmed:year1988lld:pubmed
pubmed-article:3144279pubmed:articleTitleThe structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR.lld:pubmed
pubmed-article:3144279pubmed:affiliationDept. of Chemistry, Hunter College, New York, NY.lld:pubmed
pubmed-article:3144279pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3144279pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:3144279pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed