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Literature summary for 3.2.1.17 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.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
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
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
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
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

Organism UniProt Comment Textmining
Tequatrovirus T4 P00720
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Renatured (Commentary)

Renatured (Comment) Organism
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