Ribosome exit tunnel can entropically stabilize α-helices

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 52, 2005, Pages 18956-18961

  Ziv, Guy ^a   Haran, Gilad ^a   Thirumalai, D ^b  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b Bldg 142   (United States)

Author keywords

Confinement effects; Cylindrical pores; Entropic stabilization; Folding

Indexed keywords

AMINO ACID; POLYPEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; ENTROPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; RIBOSOME; SIMULATION; TEMPERATURE; THEORY;

COMPUTER SIMULATION; ENTROPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROGEN BONDING; MODELS, STATISTICAL; MOLECULAR CONFORMATION; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES; THERMODYNAMICS;

EID: 30044447928     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0508234102     Document Type: Article

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