Results 111 to 120 of about 5,570 (173)

3D Proteomics: Structural, Functional, Chemical and Biomarker Discovery Proteomics With LiP-MS. [PDF]

Mol Cell Proteomics
Elsässer F, de Souza N, Picotti P.
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Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90. [PDF]

Bioorg Med Chem
Mansfield CR, Taggart EL, Chirgwin ME, Derbyshire ER.   +3 more
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Structure of Thermolysin

Nature New Biology, 1972
Results of the chemical and X-ray analyses are combined to locate the active site and the calcium binding sites.
B W, Matthews, P M, Colman, J N, Jansonius, K, Titani, K A, Walsh, H, Neurath   +5 more
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The unfolding mechanism of thermolysin

Biopolymers, 1983
AbstractThe ligand‐modulated kinetics of the autoproteolysis of thermolysin and the high‐molecular‐weight products of the reaction provide evidence for the conclusion that separation of the two structural domains is most probably the first step on the unfolding pathway of the protein under native conditions.
R J, Corbett, R S, Roche
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Thermolysin: A zinc metalloenzyme

Biochemical and Biophysical Research Communications, 1969
Abstract Metal analyses and inhibitor studies have shown that thermolysin, a neutral protease from B. thermoproteolyticus , is a zinc metalloenzyme. The relevance of this finding to the active site characteristics of other bacterial neutral proteases and to those of alkaline proteases is considered.
S A, Latt, B, Holmquist, B L, Vallee
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Studies on The Inhibition of Thermolysin

1976
Thei nhibition of the thermolysin catalyzed hydrolysis of FA-Gly-Leu-NH2 and FA-Gly-Phe-NH2 has been reported. The results suggest a model for substrate and inhibitor binding involving the hydrophobic specificity pocket, Arg-203 and Glu-143.
J, Feder, N, Aufderheide, B S, Wildi
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The Structure and Stability of Thermolysin

1976
Thermolysin is an extracellular proteolytic enzyme isolated from Bacillus thermoproteolyticus (Endo, 1962). The enzyme is quite thermostable, retaining over half of its activity after being heated in an aqueous solution for an hour at 80°C, while at 65°C practically no inactivation occurs (Endo, 1962; Matsubara, 1967).
L H, Weaver, W R, Kester, L F, Ten Eyck, B W, Matthews   +3 more
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Pressure dependence of thermolysin catalysis

European Journal of Biochemistry, 1984
A comparison of the pressure and temperature dependences of the catalytic reaction of thermolysin, a thermostable neutral protease from Bacillus thermoproteolyticus, with those of a non‐thermostable neutral protease from Bacillus subtilis revealed a distinct difference in Km values of these enzymes for 3‐(2‐furyl)acryloyl‐blocked dipeptide and ...
M, Fukuda, S, Kunugi
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