Functional dynamics of the hydrophobic cleft in the N-domain of calmodulin

Biophysical Journal

Volumn 80, Issue 5, 2001, Pages 2082-2092

  Vigil, Dominico ^a   Gallagher, Stephen C ^b   Trewhella, Jill ^b   García, Angel E ^a,b  

^a Theoretical Biology and Biophysics Group   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CALCIUM ION; CALMODULIN; PEPTIDE; SOLVENT;

AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CALCIUM BINDING; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; PROTEIN CONFORMATION; RADIATION SCATTERING;

EID: 0035029050     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76182-6     Document Type: Article

References (5)

1. Babu, Y., J. Sack, T. Greenhough, C. Bugg, A. Means, and W. Cook. 1985. 3-dimensional structure of calmodulin. Nature. 315:37-40.
2. Babu, Y. S., Bugg, C. E., and Cook, W. 1988. Structure of calmodulin refined at 2.2 a resolution. J. Mol. Biol. 204:191-204.
3. Barbato, G., M. Ikura, L. Kay, R. Pastor, and A. Bax. 1992. Backbone dynamics of calmodulin studied by n-15 relaxation using inverse detected 2-dimensional nmr-spectroscopy: the central helix is flexible. Biochemistry. 31:5269-5278.
4. 1H-nmr. Biochemistry. 36:11605-11618.
5. Chacon, P., J. Diaz, F. Moran, and J. Andreu. 2000. Reconstruction of protein form with x-ray solution scattering and a genetic algorithm. J. Mol. Biol. 299:1289-1302.