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The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics.
Biochemistry. 2006 Mar 14; 45(10):3412-20.B

Abstract

This paper describes the structural and dynamic properties of a hitherto uncovered alkali molten globule (MG) state of horse "ferrocytochrome c" (ferrocyt c). Several experimental difficulties mainly because of heme autoxidation and extraordinary stability of ferrocyt c have been overcome by working with the carbonmonoxide-bound molecule under extremely basic condition (pH 13) in a strictly anaerobic atmosphere. Structural and molecular properties extracted from basic spectroscopic experiments suggest that cations drive the base-denatured CO-liganded protein to the MG state. The stability of this state is approximately 5.2 kcal mol(-)(1), and the guanidinium-induced unfolding transition is sharp (m(g) approximately 2.3 kcal mol(-)(1) M(-)(1)), suggesting contents of rigid tertiary structure. Strategic experiments involving the measurement of the CO association rate to the base-denatured protein and intrachain diffusion rates measured by laser photolysis of CO indicate a substantially restricted overall motion and stiffness of the polypeptide chain in the MG state. Possible placement of the state in the folding coordinate of ferrocyt c is discussed.

Authors+Show Affiliations

School of Chemistry, University of Hyderabad, Hyderabad 500046, India.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16519536

Citation

Rao, D Krishna, et al. "The Alkali Molten Globule State of Ferrocytochrome C: Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics." Biochemistry, vol. 45, no. 10, 2006, pp. 3412-20.
Rao DK, Kumar R, Yadaiah M, et al. The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. Biochemistry. 2006;45(10):3412-20.
Rao, D. K., Kumar, R., Yadaiah, M., & Bhuyan, A. K. (2006). The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. Biochemistry, 45(10), 3412-20.
Rao DK, et al. The Alkali Molten Globule State of Ferrocytochrome C: Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics. Biochemistry. 2006 Mar 14;45(10):3412-20. PubMed PMID: 16519536.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. AU - Rao,D Krishna, AU - Kumar,Rajesh, AU - Yadaiah,M, AU - Bhuyan,Abani K, PY - 2006/3/8/pubmed PY - 2006/5/4/medline PY - 2006/3/8/entrez SP - 3412 EP - 20 JF - Biochemistry JO - Biochemistry VL - 45 IS - 10 N2 - This paper describes the structural and dynamic properties of a hitherto uncovered alkali molten globule (MG) state of horse "ferrocytochrome c" (ferrocyt c). Several experimental difficulties mainly because of heme autoxidation and extraordinary stability of ferrocyt c have been overcome by working with the carbonmonoxide-bound molecule under extremely basic condition (pH 13) in a strictly anaerobic atmosphere. Structural and molecular properties extracted from basic spectroscopic experiments suggest that cations drive the base-denatured CO-liganded protein to the MG state. The stability of this state is approximately 5.2 kcal mol(-)(1), and the guanidinium-induced unfolding transition is sharp (m(g) approximately 2.3 kcal mol(-)(1) M(-)(1)), suggesting contents of rigid tertiary structure. Strategic experiments involving the measurement of the CO association rate to the base-denatured protein and intrachain diffusion rates measured by laser photolysis of CO indicate a substantially restricted overall motion and stiffness of the polypeptide chain in the MG state. Possible placement of the state in the folding coordinate of ferrocyt c is discussed. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16519536/The_alkali_molten_globule_state_of_ferrocytochrome_c:_extraordinary_stability_persistent_structure_and_constrained_overall_dynamics_ DB - PRIME DP - Unbound Medicine ER -