Two exposed amino acid residues confer thermostability on a cold shock protein

Nature Structural Biology

Volumn 7, Issue 5, 2000, Pages 380-383

  Perl, Dieter ^a   Mueller, Uwe ^b,c   Heinemann, Udo ^b,c   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

COLD SHOCK PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLUS; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; ELECTROSTATICS; HEAT-SHOCK PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS);

EID: 0034100848     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/75151     Document Type: Article

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