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Thermal unfolding of small proteins with SH3 domain folding pattern.

Abstract:

The thermal unfolding of three SH3 domains of the Tec family of tyrosine kinases was studied by differential scanning calorimetry and CD spectroscopy. The unfolding transition of the three protein domains in the acidic pH region can be described as a reversible two-state process. For all three SH3 domains maximum stability was observed in the pH region 4.5 < pH < 7.0 where these domains unfold at temperatures of 353K (Btk), 342K (Itk), and 344K (Tec). At these temperatures an enthalpy c...

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Publication status:
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Mattson, PT More by this author
Christova, P More by this author
Berndt, KD More by this author
Karshikoff, A More by this author
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Journal:
Proteins
Volume:
31
Issue:
3
Pages:
309-319
Publication date:
1998-05-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:0739082f-8d0e-4972-ab39-6d23ae46c1e9
Source identifiers:
375460
Local pid:
pubs:375460

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