How force unfolding differs from chemical denaturation

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

Volumn 111, Issue 9, 2014, Pages 3413-3418

  Stirnemann, Guillaume ^a   Kang, Seung Gu ^b   Zhou, Ruhong ^b   Berne, Bruce J ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b IBM T J WATSON RESEARCH CENTER   (United States)

Author keywords

Atomic force microscopy; Molecular dynamics simulations; Worm like chain model

Indexed keywords

ARTICLE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ATOMIC FORCE MICROSCOPY; MOLECULAR DYNAMICS SIMULATIONS; WORM-LIKE CHAIN MODEL;

HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN UNFOLDING; UBIQUITIN; UREA;

EID: 84895812665     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1400752111     Document Type: Article

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