| pubmed-article:8218270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C1444754 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:8218270 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8218270 | pubmed:issue | 45 | lld:pubmed |
| pubmed-article:8218270 | pubmed:dateCreated | 1993-12-21 | lld:pubmed |
| pubmed-article:8218270 | pubmed:abstractText | Ala-based peptides form marginally stable helices at low temperature and are conventionally considered as mixtures of alpha-helix and random coil. However, recent work with doubly spin-labeled peptides suggests that short 16-residue sequences contain a significant fraction of 3(10)-helix near the N-terminus (positions 4-8). Using the same double-label strategy, we report on the helix geometry of the peptides Ac-(AAAAK)nA-NH2 with n = 3 and n = 4. The 16-mer (n = 3) is now examined at a region near the C-terminus, and there is evidence for 3(10)-helix here as well. The 21-mer (n = 4) is examined in three regions of the sequence. In dramatic contrast to the 16-mer, the 21-mer exhibits the signature of alpha-helix at the N-terminus and on through the middle of the peptide. The 21-mer C-terminus, however, adopts the 3(10)-helix geometry as is often found for C-termini in protein alpha-helices. These data indicate that the proportion of alpha-helix and 3(10)-helix in Ala-based peptides depends upon the sequence length. | lld:pubmed |
| pubmed-article:8218270 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8218270 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8218270 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8218270 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8218270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8218270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8218270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8218270 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8218270 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8218270 | pubmed:author | pubmed-author:MillhauserG... | lld:pubmed |
| pubmed-article:8218270 | pubmed:author | pubmed-author:MiickS MSM | lld:pubmed |
| pubmed-article:8218270 | pubmed:author | pubmed-author:FioriW RWR | lld:pubmed |
| pubmed-article:8218270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8218270 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:8218270 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8218270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8218270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8218270 | pubmed:pagination | 11957-62 | lld:pubmed |
| pubmed-article:8218270 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:meshHeading | pubmed-meshheading:8218270-... | lld:pubmed |
| pubmed-article:8218270 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8218270 | pubmed:articleTitle | Increasing sequence length favors alpha-helix over 3(10)-helix in alanine-based peptides: evidence for a length-dependent structural transition. | lld:pubmed |
| pubmed-article:8218270 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064. | lld:pubmed |
| pubmed-article:8218270 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8218270 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8218270 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8218270 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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