Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin-1

FEBS Letters

Volumn 446, Issue 1, 1999, Pages 75-80

  Dames, Sonja A ^a   Kammerer, Richard A ^a   Moskau, Detlef ^b   Engel, Jürgen ^a   Alexandrescu, Andrei T ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b Bruker AG   (Switzerland)

Author keywords

Cartilage matrix protein; Electrostatic; Ion pair; Ionization constant; Salt bridge; Specificity; Stability

Indexed keywords

MATRILIN 1; SCLEROPROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CARTILAGE MATRIX; CHICKEN; IONIZATION; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SURFACE CHARGE;

ANIMALS; ESCHERICHIA COLI; EXTRACELLULAR MATRIX PROTEINS; GLYCOPROTEINS; PROTEIN CONFORMATION;

GALLUS GALLUS;

EID: 0032984885     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00186-6     Document Type: Article

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