Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-7-20
pubmed:abstractText
It is evident that protein conformational transitions play important roles in biological machinery; however, detailed pictures of these transition processes capable of making kinetic prediction are not yet available. For a full description of these transitions, we first need to describe kinematically movements between stable states. Then, more importantly, a free energy profile associated with the conformational change needs to be obtained. Recently, a new model to describe the energy landscape of protein conformational changes was applied to the conformational transition of adenylate kinase. In this model, the conformational change coupled to the ligand binding is described as a switching between two energy surfaces that correspond to ligand bound and unbound states. The nonlinearity of the protein conformational changes is described through an iterative usage of normal mode calculations. In addition, another kind of nonlinearity enters the dynamics of the conformational transitions due to cracking, or partial unfolding, which may occur during the conformational transitions. The consequences of this theoretical model are explored in greater detail. An improved model for the cracking that includes the cooperativity of the partial unfolding in analogy to nucleation is introduced.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1959-69
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Simple energy landscape model for the kinetics of functional transitions in proteins.
pubmed:affiliation
Center for Theoretical Biological Physics and Department of Physics, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't