Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis

Proteins: Structure, Function and Genetics

Volumn 30, Issue 4, 1998, Pages 401-406

  Schindler, Thomas ^a   Perl, Dieter ^a   Graumann, Peter ^b   Sieber, Volker ^a   Marahiel, Mohamed A ^b   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Cold shock domain; Hydrophobic effect; Nucleic acid binding; Protein stability

Indexed keywords

ALANINE; BACTERIAL PROTEIN; NUCLEIC ACID; PHENYLALANINE; RIBONUCLEOPROTEIN; SOLVENT; UREA;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; COLD STRESS; HYDROPHOBICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN NUCLEIC ACID INTERACTION; PROTEIN STABILITY;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CARRIER PROTEINS; HEAT-SHOCK PROTEINS; MUTATION; NUCLEIC ACIDS; PHENYLALANINE; PROTEIN BINDING; PROTEIN CONFORMATION; RIBOSOMAL PROTEINS; RNA-BINDING PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 0032032172     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980301)30:4<401::AID-PROT7>3.0.CO;2-L     Document Type: Article

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