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Archives of Biochemistry and Biophysics

Volumn 436, Issue 2, 2005, Pages 397-405

The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive

(4) Pearson, Josh T a Dabrowski, Michael J a Kung, Irene a Atkins, William M a

a UNIVERSITY OF WASHINGTON (United States)

Author keywords

Conformational dynamics; Exo site; Protein engineering; Pyrene fluorescence; Tuberculosis

Indexed keywords

CYSTEINE; GLUTAMATE AMMONIA LIGASE; METHIONINE SULFOXIMINE; PROTEIN SUBUNIT; PYRENE DERIVATIVE;

ARTICLE; CONFORMATION; CONTROLLED STUDY; COVALENT BOND; DISULFIDE BOND; ELECTROSPRAY MASS SPECTROMETRY; ESCHERICHIA COLI; FLUORESCENCE; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; QUANTITATIVE ANALYSIS; STEADY STATE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 17744376953 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/j.abb.2005.02.008 Document Type: Article

Times cited : (8)

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