Computational design and biophysical characterization of aggregation-resistant point mutations for γd crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity

Biochemistry

Volumn 50, Issue 5, 2011, Pages 628-639

  Sahin, Erinc ^a,b   Jordan, Jacob L ^c   Spatara, Michelle L ^a   Naranjo, Andrea ^a   Costanzo, Joseph A ^c   Weiss IV, William F ^a   Robinson, Anne Skaja ^a   Fernandez, Erik J ^c   Roberts, Christopher J ^a,b  

^a University of Delaware   (United States)

^b UNIVERSITY OF DELAWARE   (United States)

^c University of Virginia   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC SOLUTIONS; AGGREGATION KINETICS; AGGREGATION PROPENSITY; BIOPHYSICAL CHARACTERIZATION; CATARACT FORMATION; CIRCULAR DICHROISM; COMPUTATIONAL DESIGN; CONFORMATIONAL STABILITIES; CRYSTALLIN; EYE-LENS PROTEIN; KINETIC MODELING; LASER LIGHT SCATTERING; MODEL SYSTEM; MULTI DOMAINS; PEPTIDE AGGREGATION; POINT MUTATIONS; SECONDARY AND TERTIARY STRUCTURES; THIOFLAVIN; WILD TYPES;

CHEMICAL STABILITY; CHROMATOGRAPHY; CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; DICHROISM; FLUORESCENCE SPECTROSCOPY; LIGHT SCATTERING;

PROTEINS;

CRYSTALLIN;

ALGORITHM; ARTICLE; CALORIMETRY; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; LIGHT SCATTERING; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; COMPUTER-AIDED DESIGN; GAMMA-CRYSTALLINS; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

EID: 79952092133     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100978r     Document Type: Article

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