Linked Life Data

19653680

Source:http://linkedlifedata.com/resource/pubmed/id/19653680

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2009-9-2
pubmed:abstractText
Internal cavities, which are central to the biological functions of myoglobin, are exploited by gaseous ligands (e.g., O(2), NO, CO, etc.) to migrate inside the protein matrix. At present, it is not clear whether the ligand makes its own way inside the protein or instead the internal cavities are an intrinsic feature of myoglobin. To address this issue, standard molecular dynamics simulations were performed on horse-heart met-myoglobin with no ligand migrating inside the protein matrix. To reveal intrinsic internal pathways, the use of a statistical approach was applied to the cavity calculation, with special emphasis on the major pathway from the distal pocket to Xe1. Our study points out the remarkable dynamical behavior of Xe4, whose "breathing motions" may facilitate migration of ligands through the distal region. Additionally, our results highlight a two-way path for a ligand to diffuse through the proximal region, possibly allowing an alternative route in case Xe1 is occupied. Finally, our approach has led us to the identification of key residues, such as leucines, that may work as switches between cavities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11825-32
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Breathing motions of a respiratory protein revealed by molecular dynamics simulations.
pubmed:affiliation
Department of Chemical Sciences, University of Cagliari, Cittadella Universitaria, I-09042 Monserrato (Ca), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't