Abnormally High pKa of an Active‐Site Glutamic Acid Residue in Bacillus Circulans Xylanase
- 1 September 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 232 (3), 839-843
- https://doi.org/10.1111/j.1432-1033.1995.0839a.x
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Mutational and crystallographic analyses of the active site residues of the bacillus circulans xylanaseProtein Science, 1994
- Stabilization of a protein by removal of unfavorable abnormal pKa: substitution of undissociable residue for glutamic acid-35 in chicken lysozymeBiochemistry, 1992
- Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35Biochemistry, 1992
- Single amino acid substitutions can further increase the stability of a thermophilic L-lactate dehydrogenaseProtein Engineering, Design and Selection, 1992
- Calorimetrically Determined Dynamics of Complex Unfolding Transitions in ProteinsAnnual Review of Biophysics, 1990
- Differential scanning calorimetry of the irreversible thermal denaturation of thermolysinBiochemistry, 1988
- New insight into protein secondary structure from resolution-enhanced infrared spectraBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Mechanism of hydrolysis by serine proteases: direct determination of the pKa's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopyBiochemistry, 1976
- Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy waterBiopolymers, 1975
- Mechanism of Lysozyme ActionScience, 1969