Linked Life Data

11749197

Source:http://linkedlifedata.com/resource/pubmed/id/11749197

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-12-25
pubmed:abstractText
We examine a minimal model for helix-forming polymers. The monomer-monomer potential energy is based on the anisotropic potentials seen in proteins and is used in conjunction with a wormlike backbone. We show that the coil-helix transition involves four states. As the temperature is lowered, the first observed state is a coil state, the second a collapsed globular, the third a highly flexible helical state, and the fourth a crystalline helical state. We discuss in detail what effect the potential energy form has on these various states by systematically varying the potential from strongly anisotropic to isotropic. The data demonstrate that the foldability of a helix is strongly related to anisotropic nature of the potential. In the isotropic case, we show that the transition following a globular collapse is not first order as postulated for these systems. In the strongly anisotropic case the globular-helix transition is consistent with cooperative first-order-like behavior.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1525-7797
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
389-401
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Helical structures in proteins.
pubmed:affiliation
Guelph-Waterloo Physics Institute, Department of Physics, University of Waterloo, Waterloo, Ontario, Canada, N2L 3G1.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't