15969539

Source:http://linkedlifedata.com/resource/pubmed/id/15969539

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0042295, umls-concept:C0162847, umls-concept:C0877853, umls-concept:C1442792, umls-concept:C1705165, umls-concept:C2700061
pubmed:issue	25
pubmed:dateCreated	2005-6-22
pubmed:abstractText	Protein folding kinetic data have been obtained for the marginally stable N-terminal SH3 domain of the Drosophila protein drk as a function of pH in order to investigate the electrostatic properties of Asp8 in the folding transition state ensemble. The slow exchange between folded and unfolded forms of the protein gives rise to separate NMR resonances for both folded and unfolded states at equilibrium. As a result, kinetic data can be derived from magnetization transfer between these two states without the need for denaturants. Using the fact that ionization of Asp8 dominates the electrostatic behavior of the protein between pH 2 and 3, along with pKa values for titrating groups in both folded and unfolded states that have been determined in a previous study, values of 2.9 +/- 0.1 and 3.3 +/- 0.2 are obtained for the pKa of Asp8 in the transition state for the wild-type protein and for a His7Ala mutant, respectively. The data are consistent with the partial formation in the transition state ensemble of an Asp8 side chain carboxylate-a Lys21 backbone amide interaction that represents a highly conserved contact in folded SH3 domains.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7503056
pubmed:citationSubset	IM
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0002-7863
pubmed:author	pubmed-author:Forman-KayJulie DJD, pubmed-author:KayLewis ELE, pubmed-author:TollingerMartinM
pubmed:issnType	Print
pubmed:day	29
pubmed:volume	127
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	8904-5
pubmed:dateRevised	2008-1-17
pubmed:meshHeading	pubmed-meshheading:15969539-Hydrogen-Ion Concentration, pubmed-meshheading:15969539-Kinetics, pubmed-meshheading:15969539-Magnetic Resonance Spectroscopy, pubmed-meshheading:15969539-Protein Folding, pubmed-meshheading:15969539-Thermodynamics, pubmed-meshheading:15969539-Time Factors
pubmed:year	2005
pubmed:articleTitle	Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
pubmed:affiliation	Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada. martin.tollinger@univie.ac.at
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't