Literature summary extracted from
Ando, N.; Barstow, B.; Baase, W.A.; Fields, A.; Matthews, B.W.; Gruner, S.M.
Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation (2008), Biochemistry, 47, 11097-11109.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.2.1.17 |
A98L |
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume |
Tequatrovirus T4 |
3.2.1.17 |
L99A |
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume |
Tequatrovirus T4 |
3.2.1.17 |
L99G/E108V |
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume |
Tequatrovirus T4 |
3.2.1.17 |
V149G |
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume |
Tequatrovirus T4 |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.17 |
Tequatrovirus T4 |
P00720 |
- |
- |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
3.2.1.17 |
study on four mutants having different cavity volumes at low and neutral pH upto a pressure of 400 MPa. The pressure-denatured state at neutral pH is even more compact than at low pH, and the preferential filling of large cavities may be responsible for the compactness. Pressure denaturation is characteristically distinct from thermal or chemical denaturation |
Tequatrovirus T4 |