Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability

This publication has 28 references indexed in Scilit:

• Theoretical Studies of the Response of a Protein Structure to Cavity-Creating Mutations
  Biophysical Journal, 2000
• ProTherm: Thermodynamic Database for Proteins and Mutants
  Nucleic Acids Research, 1999
• The stability of proteins in extreme environments
  Current Opinion in Structural Biology, 1998
• Proteins from thermophilic and mesophilic organisms essentially do not differ in packing.
  Protein Engineering, Design and Selection, 1998
• Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease
  Biochemistry, 1995
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• The Role of Interior Side-Chain Packing in Protein Folding and Stability
  Published by Springer Nature ,1994
• Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state
  Biochemistry, 1992
• Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids
  Biochemistry, 1991
• The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution
  Proteins-Structure Function and Bioinformatics, 1991