Characterization of the denaturation of human α-lactalbumin in urea by molecular dynamics simulations

Proteins: Structure, Function and Genetics

Volumn 58, Issue 2, 2005, Pages 439-449

  Smith, Lorna J ^a   Jones, Rachel M ^a   Van Gunsteren, Wilfred F ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b ETH ZURICH   (Switzerland)

Author keywords

lactalbumin; GROMOS96; MD simulations; Molten globule; Protein folding; Urea

Indexed keywords

ALPHA LACTALBUMIN; UREA; WATER;

ARTICLE; ATOM; COMPUTER SIMULATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DENATURATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLVATION; TEMPERATURE;

CIRCULAR DICHROISM; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MODELS, STATISTICAL; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTEOMICS; SOLVENTS; TEMPERATURE; THERMODYNAMICS; TIME FACTORS; UREA; WATER;

EID: 11344259541     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20287     Document Type: Article

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