Conformational changes: How small is big enough?

This publication has 24 references indexed in Scilit:

• Direct Measurement of Small Ligand-Induced Conformational Changes in the Aspartate Chemoreceptor Using EPR
  Biochemistry, 1998
• Probing the Structure of the Cytoplasmic Domain of the Aspartate Receptor by Targeted Disulfide Cross-Linking
  Biochemistry, 1997
• Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences
  Science, 1997
• Producing Positive, Negative, and No Cooperativity by Mutations at a Single Residue Located at the Subunit Interface in the Aspartate Receptor of Salmonella typhimurium
  Biochemistry, 1996
• Structural Mechanisms for Domain Movements in Proteins
  Biochemistry, 1994
• Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity
  Biochemistry, 1994
• Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a Ligand
  Science, 1991
• Space-Filling Models of Kinase Clefts and Conformation Changes
  Science, 1979
• Competitive Inhibition by Substrate during Enzyme Action. Evidence for the Induced-fit Theory^1,2
  Journal of the American Chemical Society, 1960
• ENERGY, QUANTA, AND VISION
  The Journal of general physiology, 1942