Linked Life Data

8476847

Source:http://linkedlifedata.com/resource/pubmed/id/8476847

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1993-5-25
pubmed:abstractText
Molecular dynamics simulations of apomyoglobin have been conducted in aqueous solution for 350 ps at 25 degrees C and for 500 ps in two different runs at 85 degrees C. The structures obtained at the higher temperature display properties similar to those of molten globules. Close agreement is obtained between the computed structural models and experimental data on the helical content of both native apomyoglobin and the low-pH unfolding intermediate. The results also suggest explanations for the surprising observations on the effects of mutations at the interface of the A, G, and H helices. Detailed analyses of the final structures and the unfolding pathways at high temperature clearly show that the most stable alpha-helical regions are those in contact with other helices.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4175-84
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Molecular dynamics simulations of the unfolding of apomyoglobin in water.
pubmed:affiliation
Department of Chemistry, Yale University, New Haven, Connecticut 06511.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.