Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-2-4
pubmed:abstractText
Detergent-free reaction center (RC) proteins from the photosynthetic bacterium Rhodopseudomonas viridis were obtained using Bio-Beads SM-2. With these RCs, the amount of detergent molecules associated with the protein was measured by determining the detergent concentration at which re-solubilization occurred as a function of the RC concentration. For N,N-dimethyl dodecylamine-N-oxide (LDAO), Triton X-100 and beta-octylglucoside 260 +/- 30,105 +/- 10 and 360 +/- 100 detergent molecules were necessary to dissolve the protein, respectively. With this technique we have studied the effect of the amphiphilic molecule 1,2,3-heptanetriol, which is essential in the crystallization process of these RCs. Addition of 5% 1,2,3-heptanetriol reduces the value for LDAO to 120 +/- 20 LDAO/RC, supporting the notion that crystallization of the RCs is promoted by increasing the number of protein-protein contacts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
337
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Determination of the number of detergent molecules associated with the reaction center protein isolated from the photosynthetic bacterium Rhodopseudomonas viridis. Effects of the amphiphilic molecule 1,2,3-heptanetriol.
pubmed:affiliation
Department of Biophysics, Huygens Laboratory, Leiden, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't