Stable single α-Helices are constant force springs in proteins

Journal of Biological Chemistry

Volumn 289, Issue 40, 2014, Pages 27825-27835

  Wolny, Marcin ^a   Batchelor, Matthew ^a   Knight, Peter J ^a   Paci, Emanuele ^a   Dougan, Lorna ^a   Peckham, Michelle ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CONSTANT FORCE SPRINGS;

MYOSIN; MYOSIN 10; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; IN VITRO STUDY; MOLECULAR DYNAMICS; MOLECULAR STABILITY; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN REFOLDING; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SINGLE ALPHA HELIX; ANIMAL; ATOMIC FORCE MICROSCOPY; BOVINAE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; GENETICS; METABOLISM; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

ANIMALS; CATTLE; CIRCULAR DICHROISM; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; MYOSINS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84907484123     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.585679     Document Type: Article

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