Mechanical probes of SOD1 predict systematic trends in metal and dimer affinity of ALS-associated mutants

Journal of Molecular Biology

Volumn 425, Issue 5, 2013, Pages 850-874

  Das, Atanu ^a   Plotkin, Steven S ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

ALS; molecular dynamics simulations; protein misfolding; superoxide dismutase; thermodynamic stability

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; DISULFIDE; MONOMER; MUTANT PROTEIN; ZINC;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; DEPLETION; DISULFIDE BOND; DYNAMICS; ENERGY; EQUILIBRIUM CONSTANT; GENE MUTATION; METAL BINDING; MOLECULAR STABILITY; MUTANT; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STABILITY; REDUCTION; RIGIDITY; THERMODYNAMICS; WILD TYPE;

EID: 84874109892     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.12.022     Document Type: Article

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