Contribution of active site residues to the activity and thermal stability of ribonuclease Sa

No abstract is available for this paper.

• Publication year

  2003

• Venue

  Protein Science

• Publication date

  2003-10-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1110/ps.03176803PMID 14500895PMCID PMC2366910
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2).

  2003cited by this paper
• pK values of histidine residues in ribonuclease Sa: effect of salt and net charge.

  2003cited by this paper
• Impact of enzyme motion on activity.

  2002cited by this paper
• Kinetic studies of guanine recognition and a phosphate group subsite on ribonuclease T1 using substitution mutants at Glu46 and Lys41.

  2002cited by this paper
• Analysis of catalytic residues in enzyme active sites.

  2002cited by this paper
• Structural bases of stability-function tradeoffs in enzymes.

  2002cited by this paper
• Atomic resolution data reveal flexibility in the structure of RNase Sa.

  2002cited by this paper
• The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

  2001cited by this paper
• Tyrosine hydrogen bonds make a large contribution to protein stability.

  2001cited by this paper
• Polar group burial contributes more to protein stability than nonpolar group burial.

  2001cited by this paper
• Solution structure and dynamics of ribonuclease Sa

  2001cited by this paper
• Prediction of functionally important residues based solely on the computed energetics of protein structure.

  2001cited by this paper
• Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.

  2000cited by this paper
• Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation induced cell migration.

  2000cited by this paper
• Charge–charge interactions influence the denatured state ensemble and contribute to protein stability

  2000cited by this paper
• Buried charged surface in proteins.

  2000cited by this paper
• Increasing protein stability by altering long‐range coulombic interactions

  1999cited by this paper
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  1998cited by this paper
• Electrostatic Origin of the Catalytic Power of Enzymes and the Role of Preorganized Active Sites*

  1998cited by this paper
• Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1.

  1998cited by this paper
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  1998cited by this paper
• A decade of protein engineering on ribonuclease T1--atomic dissection of the enzyme-substrate interactions.

  1997cited by this paper
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  1997cited by this paper
• Ribonuclease from Streptomyces aureofaciens at atomic resolution.

  1996cited by this paper
• A relationship between protein stability and protein function.

  1995cited by this paper
• The role of Glu-60 in the specificity of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) towards dinucleotides, poly(A) and RNA.

  1994cited by this paper
• Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate.

  1993influential reference
• Functional interactions among the His40, Glu58 and His92 catalysts of ribonuclease T1 as studied by double and triple mutants.

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• Effect of active site residues in barnase on activity and stability.

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  2017cites this paper
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  2016cites this paper
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  2015cites this paper
• Cytotoxicity of RNase Sa to the acute myeloid leukemia Kasumi-1 cells depends on the net charge

  2014cites this paper
• The Effects of Buried Ionizable Amino Acids on the Stability of Ribonuclease Sa

  2014cites this paper
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  2013cites this paper
• Identification of Chromosomal HP0892-HP0893 Toxin-Antitoxin Proteins in Helicobacter pylori and Structural Elucidation of Their Protein-Protein Interaction*

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• Molecular Structure and Function of the Novel BrnT/BrnA Toxin-Antitoxin System of Brucella abortus*

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• 1 Identification of Chromosomal HP 0892-HP 0893 Toxin-Antitoxin Proteins in Helicobacter pylori and Structural Elucidation of Their Protein-Protein Interaction *

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