Linked Life Data

20858206

Source:http://linkedlifedata.com/resource/pubmed/id/20858206

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-11-25
pubmed:abstractText
We propose a novel concept associated with the relationship between structure and function in biomolecular systems. We performed a 75 nanoseconds molecular dynamics (MD) simulation for an RNA-binding protein, neuro-oncological ventral antigen (NOVA), and examined its physico-chemical properties. NOVA dissociated from the NOVA-RNA complex showed a large conformational change: formation of intra-molecular hydrogen bonds between the C-terminal region and the loop structure located at the middle of amino acid sequence. The free energy analysis suggests that the deformed structure is more stabilized in macromolecular crowding environment where the dielectric constant is smaller than 5. The solvent accessible surface area (SASA) analysis indicates that NOVA enhances the efficiency of association with RNA by changing the relative SASA for the target sequence in RNA molecules. Based on the obtained results, we propose a novel concept of spontaneous adjustment mechanism to explain the structural and energetic changes observed for NOVA in the free state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1875-5305
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1547-52
pubmed:dateRevised
2011-3-31
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Spontaneous adjustment mechanism in an RNA-binding protein: cooperation between energetic stabilization and target search enhancement.
pubmed:affiliation
Graduate School of Engineering, Kobe University, 1-1, Rokkodai, Nada, Kobe 657-8501, Japan. kurisaki@insilico.h.kobe-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't