Linked Life Data

17046667

Source:http://linkedlifedata.com/resource/pubmed/id/17046667

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-10-18
pubmed:abstractText
Assembly of normally soluble proteins into amyloid fibrils is a cause or associated symptom of numerous human disorders. Although some progress toward understanding the molecular-level details of fibril structure has been made through in vitro experiments, the insoluble nature of fibrils make them difficult to study experimentally. We describe two computational approaches used to investigate fibril formation and structure: intermediate-resolution discontinuous molecular dynamics simulations and atomistic molecular dynamics simulations. Each method has its strengths and weaknesses, but taken together the two approaches provide a useful molecular-level picture of fibril structure and formation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
412
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
338-65
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Computational approaches to fibril structure and formation.
pubmed:affiliation
Chemical Engineering Department, North Carolina State University, Raleigh, 27695, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural