Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed α/β protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9

Journal of Molecular Biology

Volumn 289, Issue 1, 1999, Pages 167-174

  Luisi, Donna L ^a   Kuhlman, Brian ^a   Sideras, Kostandinos ^a   Evans, Philip A ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Protein folding; Ribosomal protein L9; Two state kinetics; helix

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; RIBOSOME PROTEIN;

ALPHA HELIX; AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION; CIRCULAR DICHROISM; FLUORESCENCE; GENE MUTATION; GEOBACILLUS STEAROTHERMOPHILUS; HEAT TREATMENT; KINETICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

EID: 0033612227     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2742     Document Type: Article

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