| pubmed-article:3329533 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3329533 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:3329533 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:3329533 | lifeskim:mentions | umls-concept:C0596579 | lld:lifeskim |
| pubmed-article:3329533 | lifeskim:mentions | umls-concept:C1514544 | lld:lifeskim |
| pubmed-article:3329533 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:3329533 | pubmed:dateCreated | 1988-6-20 | lld:pubmed |
| pubmed-article:3329533 | pubmed:abstractText | Membrane fluidity plays an important role in cellular functions. Membrane proteins are mobile in the lipid fluid environment; lateral diffusion of membrane proteins is slower than expected by theory, due to both the effect of protein crowding in the membrane and to constraints from the aqueous matrix. A major aspect of diffusion is in macromolecular associations: reduction of dimensionality for membrane diffusion facilitates collisional encounters, as those concerned with receptor-mediated signal transduction and with electron transfer chains. In mitochondrial electron transfer, diffusional control is prevented by the excess of collisional encounters between fast-diffusing ubiquinone and the respiratory complexes. Another aspect of dynamics of membrane proteins is their conformational flexibility. Lipids may induce the optimal conformation for catalytic activity. Breaks in Arrhenius plots of membrane-bound enzymes may be related to lipid fluidity: the break could occur when a limiting viscosity is reached for catalytic activity. Viscosity can affect protein conformational changes by inhibiting thermal fluctuations to the inner core of the protein molecule. | lld:pubmed |
| pubmed-article:3329533 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3329533 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3329533 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3329533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3329533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3329533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3329533 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3329533 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3329533 | pubmed:issn | 0144-8463 | lld:pubmed |
| pubmed-article:3329533 | pubmed:author | pubmed-author:LenazGG | lld:pubmed |
| pubmed-article:3329533 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3329533 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:3329533 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3329533 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3329533 | pubmed:pagination | 823-37 | lld:pubmed |
| pubmed-article:3329533 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:meshHeading | pubmed-meshheading:3329533-... | lld:pubmed |
| pubmed-article:3329533 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3329533 | pubmed:articleTitle | Lipid fluidity and membrane protein dynamics. | lld:pubmed |
| pubmed-article:3329533 | pubmed:affiliation | Department of Biology, University of Bologna, Italy. | lld:pubmed |
| pubmed-article:3329533 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3329533 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:3329533 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3329533 | lld:pubmed |
