Linked Life Data

17501316

Source:http://linkedlifedata.com/resource/pubmed/id/17501316

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2007-5-15
pubmed:abstractText
The mechanical unfolding of proteins is studied by extending the Wako-Saitô-Muñoz-Eaton model. This model is generalized by including an external force, and its thermodynamics turns out to be exactly solvable. We consider two molecules, the 27th immunoglobulin domain of titin and protein PIN1. We determine equilibrium force-extension curves for the titin and study the mechanical unfolding of this molecule, finding good agreement with experiments. By using an extended form of the Jarzynski equality, we compute the free energy landscape of the PIN1 as a function of the molecule length.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0031-9007
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
148102
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Ising-like model for protein mechanical unfolding.
pubmed:affiliation
Dipartimento di Fisica and CNISM, Politecnico di Torino, c. Duca degli Abruzzi 24, Torino, Italy and INFN, Sezione di Torino, Torino, Italy.
pubmed:publicationType
Journal Article