A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in γS-crystallin

Journal of Molecular Biology

Volumn 399, Issue 2, 2010, Pages 320-330

  Lee, Soojin ^a   Mahler, Bryon ^a   Toward, Jodie ^a   Jones, Blake ^a   Wyatt, Keith ^b   Dong, Lijin ^b   Wistow, Graeme ^b   Wu, Zhengrong ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b NATIONAL EYE INSTITUTE   (United States)

Author keywords

Amyloid; Cataract; Denaturation; H D exchange; S crystallin

Indexed keywords

AMYLOID; DEUTERIUM; GAMMA CRYSTALLIN; GUANIDINE; HYDROGEN; MUTANT PROTEIN; THIOFLAVINE;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; ATOMIC FORCE MICROSCOPY; CARBOXY TERMINAL SEQUENCE; CELL FUNCTION; EQUILIBRIUM CONSTANT; ION EXCHANGE; LENS; MOUSE; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; ROOM TEMPERATURE; STRESS;

VERTEBRATA;

EID: 77953082435     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.003     Document Type: Article

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