Linked Life Data

10966784

Source:http://linkedlifedata.com/resource/pubmed/id/10966784

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-9-21
pubmed:abstractText
The stepwise tryptic degradation of the interconverting quaternary isoforms of seminal ribonuclease has been analysed by structural modelling, based on the experimental results obtained by treating the dimeric protein with trypsin. The results of the analysis were compared with those obtained applying to the action of trypsin on seminal ribonuclease a recently proposed predictive algorithm for limited proteolysis. The attention was focussed on the MxM form of the protein, in which the two subunits swap their N-terminal ends interconverting at equilibrium with the M=M form with no interchange between subunits. The analysis led to the identification of a key intermediate in the interconversion pathway, and to the resolution of the apparent contradiction between prediction and actual experimental data.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
301
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
775-82
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The interconversion of isoforms of seminal ribonuclease: modelling key intermediates and trypsin effects.
pubmed:affiliation
Dipartimento di Chimica Organica e Biologica, Universita' di Napoli Federico II, Via Mezzocannone 16, Napoli, 80134, Italy.
pubmed:publicationType
Journal Article