15N nuclear magnetic resonance relaxation studies on rat β-parvalbumin and the pentacarboxylate variants, S55D and G98D-Reference-Cited by-同舟云学术

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15N nuclear magnetic resonance relaxation studies on rat β-parvalbumin and the pentacarboxylate variants, S55D and G98D

Published:2009-04-13 Issue:1 Volume:11 Page:158-173
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Henzl Michael T.,Wycoff Wei G.,Larson John D.,Likos John J.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference71 articles.

1. Refinement of recombinant oncomodulin at 1.30 A resolution;Ahmed;J. Mol. Biol.,1993

2. Effects of ion binding on the backbone dynamics of calbindin D9k determined by 15N NMR relaxation;Akke;Biochemistry,1993a

3. NMR order parameters and free energy: An analytical approach and its application to cooperative Ca2+ binding to calbindin D9k;Akke;J. Am. Chem. Soc.,1993b

4. 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins;Baldellon;Biochemistry,1998

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