Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature

Proteins: Structure, Function and Genetics

Volumn 71, Issue 3, 2008, Pages 1123-1133

  Kumar, Niti ^a   Shukla, Swati ^a   Kumar, Sanjiv ^a   Suryawanshi, Anju ^a   Chaudhry, Uma ^a   Ramachandran, Srinivasan ^a   Maiti, Souvik ^a  

^a CSIR INSTITUTE OF GENOMICS AND INTEGRATIVE BIOLOGY   (India)

Author keywords

Biotin binding; Disordered; Spectroscopy; Unfolded

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; BIOTIN; CONGO RED; HISTIDINE; RV3221C PROTEIN; THIOFLAVINE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; HIGH TEMPERATURE; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEFECT; PROTEIN FOLDING; PROTEIN STRUCTURE; TURBIDITY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOTIN; BODY TEMPERATURE; HEAT; HISTIDINE; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING;

EUKARYOTA; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

EID: 42449154662     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21798     Document Type: Article

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