Molecular crowding enhances native structure and stability of α/β protein flavodoxin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 48, 2007, Pages 18976-18981

  Stagg, Loren ^a   Zhang, Shao Qing ^b   Cheung, Margaret S ^b   Wittung Stafshede, Pernilla ^a  

^a RICE UNIVERSITY   (United States)

^b University of Houston   (United States)

Author keywords

Energy landscape theory; Excluded volume effect; Molecular simulations; Protein folding

Indexed keywords

FICOLL; FLAVODOXIN;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONTROLLED STUDY; DESULFOVIBRIO DESULFURICANS; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; THERMOSTABILITY;

APOPROTEINS; BUFFERS; CIRCULAR DICHROISM; COMPUTER SIMULATION; DESULFOVIBRIO DESULFURICANS; FICOLL; FLAVODOXIN; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

DESULFOVIBRIO DESULFURICANS;

EID: 37649016316     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0705127104     Document Type: Article

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