The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.
The amide hydrogen-deuterium exchange (HX) in the Src homology region 3 (SH3) domain of alpha-spectrin has been measured by nuclear magnetic resonance as a function of temperature between 8 and 46 degrees 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.
Sadqi
M
M
Departamento de Qui;mica Fi;sica e Instituto de Biotecnologi;a, Facultad de Ciencias, Universidad de Granada, 18071, Granada, Spain. conejero@ugr.es
Casares
S
S
López-Mayorga
O
O
Conejero-Lara
F
F
D003903:Deuterium / Q000737:chemistry / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism*; D013049:Spectrin / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics; D018909:src Homology Domains
D013049:Spectrin; D006859:Hydrogen; D003903:Deuterium