The folding cooperativity of a protein is controlled by its chain topology

Nature

Volumn 465, Issue 7298, 2010, Pages 637-640

  Shank, Elizabeth A ^a,b,c   Cecconi, Ciro ^a,b,d   Dill, Jesse W ^a,b   Marqusee, Susan ^a,b   Bustamante, Carlos ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIGOXIGENIN; DISULFIDE; LYSOZYME; POLYPEPTIDE; POLYSTYRENE; T4 LYSOZYME; UNCLASSIFIED DRUG;

CATALYSIS; ENZYME; MOLECULAR ANALYSIS; OPTICAL METHOD; PEPTIDE; PROTEIN;

ARTICLE; CONTROLLED STUDY; FORCE; OPTICAL TWEEZERS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN VARIANT;

ALLOSTERIC REGULATION; BACTERIOPHAGE T4; MODELS, MOLECULAR; MUTANT PROTEINS; OPTICAL TWEEZERS; PROBABILITY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; VIRAL PROTEINS;

EID: 77953231020     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09021     Document Type: Article

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