| pubmed-article:1793814 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0028954 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0302523 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0700325 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0699759 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C1882348 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:1793814 | lifeskim:mentions | umls-concept:C0045888 | lld:lifeskim |
| pubmed-article:1793814 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:1793814 | pubmed:dateCreated | 1992-4-3 | lld:pubmed |
| pubmed-article:1793814 | pubmed:abstractText | The solution conformation of peptides rich in the alpha, alpha-dialkylated amino acid Aib has proven to be a subtle problem, not because of helix/coil transitions, but rather because of alpha-helical/3(10)-helical competition. A special series of peptides containing 75% Aib has been synthesized that feature identical amino acid composition but differing sequences; they are sequence permutation isomers. Nuclear magnetic resonance hydrogen-bonding studies reveal that there is a sequence permutation induced transition between the two alternative helical forms within this set. The implications for the design and conformational prediction of helical Aib-rich peptides are discussed. | lld:pubmed |
| pubmed-article:1793814 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793814 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1793814 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793814 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1793814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793814 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1793814 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1793814 | pubmed:issn | 0006-3525 | lld:pubmed |
| pubmed-article:1793814 | pubmed:author | pubmed-author:BataJJ | lld:pubmed |
| pubmed-article:1793814 | pubmed:author | pubmed-author:BagchiKK | lld:pubmed |
| pubmed-article:1793814 | pubmed:author | pubmed-author:KukiAA | lld:pubmed |
| pubmed-article:1793814 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1793814 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:1793814 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1793814 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1793814 | pubmed:pagination | 1763-74 | lld:pubmed |
| pubmed-article:1793814 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:meshHeading | pubmed-meshheading:1793814-... | lld:pubmed |
| pubmed-article:1793814 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1793814 | pubmed:articleTitle | Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. I. Observation of a 3(10)/alpha-helical transition upon sequence permutation. | lld:pubmed |
| pubmed-article:1793814 | pubmed:affiliation | Cornell University, Department of Chemistry, Baker Laboratory, Ithaca, New York 14853. | lld:pubmed |
| pubmed-article:1793814 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1793814 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1793814 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1793814 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1793814 | lld:pubmed |
