Distinct structural changes detected by x-ray fiber diffraction in stabilization of F-actin by lowering pH and increasing ionic strength

Biophysical Journal

Volumn 80, Issue 2, 2001, Pages 841-851

  Oda, Toshiro ^a,b,d   Makino, Kouji ^a,b   Yamashita, Ichiro ^a   Namba, Keiichi ^a,c   Maéda, Yuichiro ^a,b  

^a ADVANCED TELECOMMUNICATIONS RESEARCH INSTITUTE INTERNATIONAL   (Japan)

^b RIKEN HARIMA INSTITUTE   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL BOND; CONFORMATIONAL TRANSITION; NONHUMAN; PH; POLYMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; X RAY DIFFRACTION;

ANIMALIA;

EID: 0035143042     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76063-8     Document Type: Article

References (3)

1. Belmont, L. D., and D. G. Drubin. 1998. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J Cell Biol. 142:1289-1299.
2. Bremer, A., R. C. Millonig, R. Sütterlin, A. Engel, T. D. Pollard, and U. Aebi. 1991. The structural basis for the intrinsic disorder of actin filament: the "lateral slipping" model. J. Cell Biol. 115:689-703.
3. Carlier, M. F. 1991. Actin: protein structure and filament dynamics. J. Biol. Chem. 266:1-4.