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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4859
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pubmed:dateCreated |
1988-7-15
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases A,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Flavodoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Myoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Polypeptide,
http://linkedlifedata.com/resource/pubmed/chemical/Parvalbumins,
http://linkedlifedata.com/resource/pubmed/chemical/Plastocyanin,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Scorpion Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrahydrofolate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Triose-Phosphate Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/pancreatic polypeptide, avian
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
240
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1632-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2837824-Amino Acid Sequence,
pubmed-meshheading:2837824-Animals,
pubmed-meshheading:2837824-Carboxypeptidases,
pubmed-meshheading:2837824-Carboxypeptidases A,
pubmed-meshheading:2837824-Cytochrome c Group,
pubmed-meshheading:2837824-Flavodoxin,
pubmed-meshheading:2837824-Humans,
pubmed-meshheading:2837824-Hydrogen Bonding,
pubmed-meshheading:2837824-Models, Chemical,
pubmed-meshheading:2837824-Molecular Sequence Data,
pubmed-meshheading:2837824-Muramidase,
pubmed-meshheading:2837824-Myoglobin,
pubmed-meshheading:2837824-Pancreatic Polypeptide,
pubmed-meshheading:2837824-Parvalbumins,
pubmed-meshheading:2837824-Plastocyanin,
pubmed-meshheading:2837824-Protein Conformation,
pubmed-meshheading:2837824-Ribonucleases,
pubmed-meshheading:2837824-Scorpion Venoms,
pubmed-meshheading:2837824-Tetrahydrofolate Dehydrogenase,
pubmed-meshheading:2837824-Triose-Phosphate Isomerase,
pubmed-meshheading:2837824-Trypsin Inhibitors,
pubmed-meshheading:2837824-X-Ray Diffraction
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pubmed:year |
1988
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pubmed:articleTitle |
Helix signals in proteins.
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pubmed:affiliation |
Department of Biological Chemistry, Hershey Medical Center, Pennsylvania State University, Hershey 17033.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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