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The temperature dependence of the hydrogen exchange in the SH3 domain of α‐spectrin
Author(s) -
Sadqi M.,
Casares S.,
López-Mayorga O.,
Conejero-Lara F.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03172-1
Subject(s) - chemistry , spectrin , enthalpy , sh3 domain , deuterium , amide , thermodynamics , crystallography , physics , proto oncogene tyrosine protein kinase src , atomic physics , biochemistry , kinase , cytoskeleton , cell
The amide hydrogen–deuterium exchange (HX) in the Src homology region 3 (SH3) domain of α‐spectrin has been measured by nuclear magnetic resonance as a function of temperature between 8 and 46°C. The analysis of the temperature dependence of HX from a statistical thermodynamic point of view has allowed us to estimate the enthalpies and entropies of the conformational processes leading to HX. The results indicate that under native conditions the domain undergoes a wide variety of conformational fluctuations, ranging from local motions, mainly located in loops, turns and chain ends and involving only low enthalpy and entropy, to extensive structural disruptions affecting its core and involving enthalpies and entropies that come fairly close to those observed during global unfolding.