| pubmed-article:2837824 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2837824 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:2837824 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2837824 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:2837824 | pubmed:issue | 4859 | lld:pubmed |
| pubmed-article:2837824 | pubmed:dateCreated | 1988-7-15 | lld:pubmed |
| pubmed-article:2837824 | pubmed:abstractText | The alpha helix, first proposed by Pauling and co-workers, is a hallmark of protein structure, and much effort has been directed toward understanding which sequences can form helices. The helix hypothesis, introduced here, provides a tentative answer to this question. The hypothesis states that a necessary condition for helix formation is the presence of residues flanking the helix termini whose side chains can form hydrogen bonds with the initial four-helix greater than N-H groups and final four-helix greater than C-O groups; these eight groups would otherwise lack intrahelical partners. This simple hypothesis implies the existence of a stereochemical code in which certain sequences have the hydrogen-bonding capacity to function as helix boundaries and thereby enable the helix to form autonomously. The three-dimensional structure of a protein is a consequence of the genetic code, but the rules relating sequence to structure are still unknown. The ensuing analysis supports the idea that a stereochemical code for the alpha helix resides in its boundary residues. | lld:pubmed |
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| pubmed-article:2837824 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2837824 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2837824 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2837824 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2837824 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2837824 | pubmed:author | pubmed-author:RossG RGR | lld:pubmed |
| pubmed-article:2837824 | pubmed:author | pubmed-author:PrestaL GLG | lld:pubmed |
| pubmed-article:2837824 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2837824 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:2837824 | pubmed:volume | 240 | lld:pubmed |
| pubmed-article:2837824 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2837824 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2837824 | pubmed:pagination | 1632-41 | lld:pubmed |
| pubmed-article:2837824 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2837824 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2837824 | pubmed:articleTitle | Helix signals in proteins. | lld:pubmed |
| pubmed-article:2837824 | pubmed:affiliation | Department of Biological Chemistry, Hershey Medical Center, Pennsylvania State University, Hershey 17033. | lld:pubmed |
| pubmed-article:2837824 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2837824 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2837824 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2837824 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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