Linked Life Data

9116018

Source:http://linkedlifedata.com/resource/pubmed/id/9116018

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1997-4-21
pubmed:abstractText
Previous studies have produced conflicting interpretations regarding the aggregation state of BPTI in solution. Here, pulsed-field gradient NMR self-association measurements have been performed with BPTI under a variety of temperature, pH, salt, urea conditions, and protein concentrations. Relative to the standard proteins, lysozyme, ribonuclease, and ubiquitin, diffusion constants indicate that BPTI dimerizes at concentrations above about 3 mg/mL and below 280 K. At higher temperatures, a marked self-association is observed above 10 mg/mL. The apparent lack of significant effects from variations in pH and NaCl concentration suggests minimal contribution to the aggregation process from charge-charge interactions. In contrast, in nondenaturing concentrations of urea (2 M), BPTI behaves as a monomer, suggesting that hydrophobic and polar residues modulate BPTI association. The BPTI surface shows that while one side is highly charged, the opposite side, composed mostly of hydrophobic and some hydrophilic residues, is feasible as an interface for BPTI self-association.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3383-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.
pubmed:affiliation
Department of Biochemistry, Health Sciences Center, University of Minnesota, Twin Cities 55455, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.