Steady-state and time-resolved fluorescence studies on wild type and mutant Chromatium vinosum high potential iron proteins: Holo- and apo-forms

Biophysical Journal

Volumn 81, Issue 4, 2001, Pages 2320-2330

  Sau, Apurba K ^a   Chen, Chun An ^b   Cowan, James A ^b   Mazumdar, Shyamalava ^a   Mitra, Samaresh ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; IRON SULFUR PROTEIN; TRYPTOPHAN;

ARTICLE; BACTERIUM MUTANT; CHROMATIUM VINOSUM; CIRCULAR DICHROISM; CONTROLLED STUDY; ENERGY TRANSFER; ENTROPY; FLUORESCENCE; HYDROPHOBICITY; MATHEMATICAL ANALYSIS; MOLECULAR MODEL; NONHUMAN; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLVATION; STEADY STATE; TIME; WAVEFORM;

ALLOCHROMATIUM VINOSUM; BACTERIA (MICROORGANISMS); CHROMATIUM; CHROMATIUM VINOSUM;

EID: 0034809210     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75878-X     Document Type: Article

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