Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge-charge interactions

Protein Science

Volumn 16, Issue 12, 2007, Pages 2694-2702

  Schweiker, Katrina L ^a,b   Zarrine Afsar, Arash ^c   Davidson, Alan R ^c   Makhatadze, George I ^b  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

^b RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Charge charge interactions; Protein stability; Protein surface; Rational design

Indexed keywords

AMINO ACID; ISOPROTEIN; PROTEIN KINASE FYN; PROTEIN SH3;

ALGORITHM; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CHICKEN; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY METABOLISM; MELTING POINT; MOLECULAR INTERACTION; PREDICTION; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN VARIANT; SURFACE CHARGE; THEORETICAL STUDY; THERMODYNAMICS; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CHICKENS; CIRCULAR DICHROISM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-FYN; SEQUENCE ALIGNMENT; THERMODYNAMICS; TRANSITION TEMPERATURE;

EID: 36448996957     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073091607     Document Type: Article

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