Linked Life Data

9315865

Source:http://linkedlifedata.com/resource/pubmed/id/9315865

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
1997-10-23
pubmed:abstractText
The in situ aggregational behavior of the bacteriophage M13 major coat protein was determined for the protein isolated in sodium cholate and reconstituted into DOPC lipid bilayers. For this purpose, the cysteine mutants A49C and T36C of the major coat protein were labeled with either a maleimido spin-label or a fluorescence label (IAEDANS). The steric restrictions sensed by the spin-label were used to evaluate the local protein conformation and the extent of protein-protein interactions at the position of the labeled residue. In addition, fluorescent labels covalently attached to the protein were used to determine the polarity of the local environment. The labeled coat protein mutants were examined under different conditions of protein association (amphiphile environment, ionic strength, temperature, and pH). The aggregational state of the major coat protein solubilized from the phage particle in sodium cholate was not dependent on the ionic strength, but was strongly dependent on cholate concentration and pH during sample preparation. At pH 7.0 and high sodium cholate concentration, the protein was in a dimeric form. The unusually strong association properties of the protein dimer in sodium cholate at pH 7.0 were attributed to the inability of sodium cholate to disrupt the strong hydrophobic forces between neighboring protein subunits in the phage particle. Such a "structural protein dimer" was, however, completely and irreversibly disrupted at pH 10.0. Qualitatively the same aggregational tendency was found upon changing the pH for the coat protein reconstituted in DOPC lipid bilayers. This reveals that the dimer disruption process is primarily a protein property, because there are no titratable groups on DOPC in the experimental pH range. The results are interpreted in terms of a model relating the protein aggregational state in the assembled phage to the protein aggregational behavior in sodium cholate and lipid bilayers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12268-75
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9315865-Bacteriophage M13, pubmed-meshheading:9315865-Capsid, pubmed-meshheading:9315865-Capsid Proteins, pubmed-meshheading:9315865-Chemistry, Physical, pubmed-meshheading:9315865-Cholic Acid, pubmed-meshheading:9315865-Cholic Acids, pubmed-meshheading:9315865-Circular Dichroism, pubmed-meshheading:9315865-Cross-Linking Reagents, pubmed-meshheading:9315865-Electron Spin Resonance Spectroscopy, pubmed-meshheading:9315865-Fluorescent Dyes, pubmed-meshheading:9315865-Lipid Bilayers, pubmed-meshheading:9315865-Membrane Proteins, pubmed-meshheading:9315865-Naphthalenesulfonates, pubmed-meshheading:9315865-Physicochemical Phenomena, pubmed-meshheading:9315865-Protein Structure, Secondary, pubmed-meshheading:9315865-Spectrometry, Fluorescence, pubmed-meshheading:9315865-Spin Labels
pubmed:year
1997
pubmed:articleTitle
In situ aggregational state of M13 bacteriophage major coat protein in sodium cholate and lipid bilayers.
pubmed:affiliation
Department of Molecular Physics, Wageningen Agricultural University, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't