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Volumn 40, Issue 9, 2001, Pages 2723-2731

Direct comparison of experimental and calculated folding free energies for hydrophobic deletion mutants of chymotrypsin inhibitor 2: Free energy perturbation calculations using transition and denatured states from molecular dynamics simulations of unfolding

(2) Pan, Y P a Daggett, V a

a UNIVERSITY OF WASHINGTON (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN INHIBITOR; CHYMOTRYPSIN INHIBITOR 2; UNCLASSIFIED DRUG;

ARTICLE; CALCULATION; CONTROLLED STUDY; ENERGY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ALANINE; AMINO ACID SUBSTITUTION; CHYMOTRYPSIN; COMPUTER SIMULATION; GLYCINE; HORDEUM; ISOLEUCINE; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; REPRODUCIBILITY OF RESULTS; SERINE PROTEINASE INHIBITORS; THERMODYNAMICS; VALINE;

EID: 0035814880 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0022036 Document Type: Article

Times cited : (40)

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