Linked Life Data

9079357

Source:http://linkedlifedata.com/resource/pubmed/id/9079357

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-4-25
pubmed:abstractText
It is argued that the chemical nature of the polypeptide backbone is the central determinant of the three-dimensional structures of proteins. The requirement that buried polar groups form intramolecular hydrogen bonds limits the fold of the backbone to the well known units of secondary structure while the amino acid sequence chooses among the set of conformations available to the backbone. 'Sidechain-only' models, based for example on hydrophobicity patterns, fail to account for the properties of the backbone and thus will have difficulty capturing essential features of a folding pathway. This is evident from the incorrect predictions they make for the conformations of the limiting cases of all-hydrophobic or all-polar sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1359-0278
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
R17-20
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Adding backbone to protein folding: why proteins are polypeptides.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. Honig@Bass.Bioc.Columbia.Edu
pubmed:publicationType
Journal Article, Review