Linked Life Data

2177662

Source:http://linkedlifedata.com/resource/pubmed/id/2177662

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1991-3-13
pubmed:abstractText
The hydrodynamics of the bacterial elongation factor EF-Tu have been studied in the presence of its ligand guanosine-5'-diphosphate (GDP) by sedimentation in the ultracentrifuge and quasielastic light scattering. Sedimentation studies have made it possible to establish experimental conditions under which only negligible aggregation of the protein occurs (neutral pH, concentration less than 3 mg/mL). Analysis of the light intensity autocorrelation functions under these conditions revealed two independent scattering species with diffusion coefficients of 0.71 X 10(-6) and 0.04 X 10(-6) cm2 s-1. The material with the lower diffusion coefficient, i.e., the aggregates, represented less than 1% of the total number of EF-Tu particles. The other 99% diffused as monomeric molecules with a molar mass corresponding to the value calculated from the known primary structure of the protein. The hydrodynamic parameters derived from the experimental data suggest that EF-Tu.GDP in solution is close to a spherical particle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-308
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
A hydrodynamic study with quasielastic light scattering and sedimentation of bacterial elongation factor EF-Tu.guanosine-5'-diphosphate complex under nonassociating conditions.
pubmed:affiliation
Department of Physical and Macromolecular Chemistry, Gorlaeus Laboratories, Leiden University, The Netherlands.
pubmed:publicationType
Journal Article