Linked Life Data

8968566

Source:http://linkedlifedata.com/resource/pubmed/id/8968566

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-4-7
pubmed:abstractText
Molecular dynamics simulations have been used to investigate the behavior of the peripheral membrane protein, cytochrome c, covalently tethered to hydrophobic (methyl-terminated) and hydrophilic (thiol-terminated) self-assembled monolayers (SAMs). The simulations predict that the protein will undergo minor structural changes when it is tethered to either surface, and the structures differ qualitatively on the two surfaces: the protein is less spherical on the hydrophilic SAM where the polar surface residues reach out to interact with the SAM surface. The protein is completely excluded from the hydrophobic SAM but partially dissolves in the hydrophilic SAM. Consequently, the surface of the thiol-terminated SAM is considerably less ordered than that of the methyl-terminated SAM, although a comparable, high degree of order is maintained in the bulk of both SAMs: the chains exhibit collective tilts in the nearest-neighbor direction at angles of 20 degrees and 17 degrees with respect to the surface normal in the hydrophobic and the hydrophilic SAMs, respectively. On the hydrophobic SAM the protein is oriented so that the heme plane is more nearly parallel to the surface, whereas on the hydrophilic surface it is more nearly perpendicular. The secondary structure of the protein, dominated by alpha helices, is not significantly affected, but the structure of the loops as well as the helix packing is slightly modified by the surfaces.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2933-41
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Molecular dynamics simulations of a protein on hydrophobic and hydrophilic surfaces.
pubmed:affiliation
Department of Chemistry, University of Pennsylvania, Philadelphia 19104-6323, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.