Linked Life Data

11842218

Source:http://linkedlifedata.com/resource/pubmed/id/11842218

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-2-20
pubmed:abstractText
Biological water at the interface of proteins is critical to their equilibrium structures and enzyme function and to phenomena such as molecular recognition and protein-protein interactions. To actually probe the dynamics of water structure at the surface, we must examine the protein itself, without disrupting the native structure, and the ultrafast elementary processes of hydration. Here we report direct study, with femtosecond resolution, of the dynamics of hydration at the surface of the enzyme protein Subtilisin Carlsberg, whose single Trp residue (Trp-113) was used as an intrinsic biological fluorescent probe. For the protein, we observed two well separated dynamical solvation times, 0.8 ps and 38 ps, whereas in bulk water, we obtained 180 fs and 1.1 ps. We also studied a covalently bonded probe at a separation of approximately 7 A and observed the near disappearance of the 38-ps component, with solvation being practically complete in (time constant) 1.5 ps. The degree of rigidity of the probe (anisotropy decay) and of the water environment (protein vs. micelle) was also studied. These results show that hydration at the surface is a dynamical process with two general types of trajectories, those that result from weak interactions with the selected surface site, giving rise to bulk-type solvation (approximately 1 ps), and those that have a stronger interaction, enough to define a rigid water structure, with a solvation time of 38 ps, much slower than that of the bulk. At a distance of approximately 7 A from the surface, essentially all trajectories are bulk-type. The theoretical framework for these observations is discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-10423454, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-11325713, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-11752400, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-1585178, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-1856864, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-1948083, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-3741490, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-7858139, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-8297378, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-8539602, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-8816770, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-9482874, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-9649375, http://linkedlifedata.com/resource/pubmed/commentcorrection/11842218-9789015
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1763-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution.
pubmed:affiliation
Laboratory for Molecular Sciences, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.