pubmed-article:7664050 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7664050 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
pubmed-article:7664050 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
pubmed-article:7664050 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:7664050 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
pubmed-article:7664050 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:7664050 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7664050 | pubmed:dateCreated | 1995-10-10 | lld:pubmed |
pubmed-article:7664050 | pubmed:abstractText | Arginine is a stabilizing element in both thermophilic and low molecular weight proteins. Similarly Lys+-->Arg+ substitutions increase the helix content of designed helical peptides. Here we explore this 'arginine effect' by examining how Lys+-->Arg+ substitutions influence the 3(10)-helix-->alpha-helix equilibrium in the helical peptide Ac-(AAAAK)3A-NH2. The unsubstituted sequence contains a significant amount of 3(10)-helix, however, single Lys+-->Arg+ substitutions shift the peptide conformation toward alpha-helix in a position-dependent fashion. The single substitution closest to the carboxy terminus induces the largest conformational change at the helix amino terminus. These findings suggest that a single strategically-placed arginine can exert long range control on helix structure. | lld:pubmed |
pubmed-article:7664050 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:language | eng | lld:pubmed |
pubmed-article:7664050 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7664050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7664050 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7664050 | pubmed:month | Jun | lld:pubmed |
pubmed-article:7664050 | pubmed:issn | 1072-8368 | lld:pubmed |
pubmed-article:7664050 | pubmed:author | pubmed-author:MillhauserG... | lld:pubmed |
pubmed-article:7664050 | pubmed:author | pubmed-author:FioriW RWR | lld:pubmed |
pubmed-article:7664050 | pubmed:author | pubmed-author:LundbergK MKM | lld:pubmed |
pubmed-article:7664050 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7664050 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:7664050 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7664050 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7664050 | pubmed:pagination | 374-7 | lld:pubmed |
pubmed-article:7664050 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:meshHeading | pubmed-meshheading:7664050-... | lld:pubmed |
pubmed-article:7664050 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7664050 | pubmed:articleTitle | A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide. | lld:pubmed |
pubmed-article:7664050 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA. | lld:pubmed |
pubmed-article:7664050 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7664050 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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