Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-8-22
pubmed:abstractText
A persistent discrepancy exists between theoretical predictions and experimental observations for the diffusion coefficients of integral membrane proteins in lipid bilayers free of immobilized proteins. Current thermodynamic theories overestimate tracer diffusion coefficients at high area fractions. We explore the hypothesis that the combined effect of hydrodynamic and thermodynamic interactions reconciles theory with experiment. We have determined previously the short- and long-time tracer diffusivities, Ds and Dl, respectively, of integral membrane proteins in lipid bilayers as a function of their area fraction, phi. The results are based on two-particle hydrodynamic and thermodynamic interactions and are precise to O(phi). Here we extend the results for Dl to high phi by combining the hydrodynamic results for Ds into theories for Dl based on many-particle thermodynamic interactions. The results compare favorably with the experimental measurements of Dl as a function of protein area fraction for bacteriorhodopsin in reconstituted membranes and for complex III of the mitochondrial inner membrane. The agreement suggests that both hydrodynamic and thermodynamic interactions are important determinants of diffusion coefficients of proteins in lipid bilayers. Additional experiments are required to verify the role of hydrodynamic interactions in protein diffusion in reconstituted systems.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-1059096, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-1161000, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-2720074, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-2720077, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-2775829, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-2956429, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-3170548, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-3427202, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-4333397, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-6184082, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-6290668, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-6940124, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-6956861, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-6956904, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-7199052, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-7284552, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-7612825, http://linkedlifedata.com/resource/pubmed/commentcorrection/7612824-786399
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1828-35
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Effect of hydrodynamic interactions on the diffusion of integral membrane proteins: tracer diffusion in organelle and reconstituted membranes.
pubmed:affiliation
School of Chemical Engineering, Cornell University, Ithaca, New York 14853, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.