Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone.
Scott-Ward, Toby S
Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone. [electronic resource] - The FEBS journal Dec 2009 - 7097-109 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1742-4658
10.1111/j.1742-4658.2009.07421.x doi
Animals
Binding Sites
Cystic Fibrosis Transmembrane Conductance Regulator--chemistry
HSC70 Heat-Shock Proteins--chemistry
Humans
Mice
Phenylalanine--genetics
Protein Conformation
Protein Folding
Protein Structure, Tertiary
Structure-Activity Relationship
Surface Plasmon Resonance
Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone. [electronic resource] - The FEBS journal Dec 2009 - 7097-109 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1742-4658
10.1111/j.1742-4658.2009.07421.x doi
Animals
Binding Sites
Cystic Fibrosis Transmembrane Conductance Regulator--chemistry
HSC70 Heat-Shock Proteins--chemistry
Humans
Mice
Phenylalanine--genetics
Protein Conformation
Protein Folding
Protein Structure, Tertiary
Structure-Activity Relationship
Surface Plasmon Resonance