Results 121 to 130 of about 5,570 (173)

Amino-acid Sequence of Thermolysin

Nature New Biology, 1972
The following three articles describe how chemical and X-ray analyses have been combined to elucidate the structure of thermolysin. This first article describes the determination of the amino-acid sequence of this metalloendopeptidase.
K, Titani, M A, Hermodson, L H, Ericsson, K A, Walsh, H, Neurath   +4 more
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The thermodynamics of calcium binding to thermolysin

Biophysical Chemistry, 1986
Calcium binding isotherms were determined for thermolysin in the range pH 5.6-10.5, and from 5 to 45 degrees C. An extensive statistical analysis of the binding data suggests that at least two of the four binding sites bind Ca2+ with complete positive cooperativity and independently of the other two.
J D, Buchanan, R J, Corbett, R S, Roche
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Thermolysin: Kinetic Study with Oligopeptides

European Journal of Biochemistry, 1970
Thermolysin is a well‐known protease which exhibits its specificity against hydrophobic amino acid residues such as l‐leucine, l‐phenylalanine, etc. whose amino groups donate the susceptible peptide bonds (amino‐endopeptidase). The present study was undertaken to investigate the effects of neighboring residues surrounding the sensitive amino acid ...
K, Morihara, H, Tsuzuki
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Three-dimensional Structure of Thermolysin

Nature New Biology, 1972
The electron density map of thermolysin indicates how the polypeptide chain is displaced throughout the overall shape of the molecule.
B W, Matthews, J N, Jansonius, P M, Colman, B P, Schoenborn, D, Dupourque   +4 more
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Silanediol-Based inhibitor of thermolysin

Bioorganic & Medicinal Chemistry Letters, 2002
The first silanediol inhibitor of thermolysin is reported, prepared by analogy with the Grobelny/Bartlett phosphinate inhibitor. A Cbz group on nitrogen proved to be unstable to the triflic acid mediated silanediol deprotection and was replaced with a dihydrocinnamoyl group.
Jaeseung, Kim, Athanasios, Glekas, Scott, McN Sieburth   +2 more
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Peptide synthesis with halophenylalanines by thermolysin

Applied Microbiology and Biotechnology, 1994
Thermolysin was able to catalyze enantioselective peptide synthesis with non-natural amino acids, halophenylalanines. However, the reactivity of thermolysin was considerably influenced by the kind and position of halogen substituents on these analogues.
Y, Imaoka, T, Kawamoto, M, Ueda, A, Tanaka   +3 more
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Inhibition of thermolysin with nitrone-bearing substrate analogs: A new type of thermolysin inhibitors

Bioorganic & Medicinal Chemistry Letters, 1998
Nitrones are utilized as the active site zinc coordinating functionality in the design of inhibitors for thermolysin. This new type of thermolysin inhibitors are as potent as the existing inhibitors bearing a carboxylate or hydroxamate zinc ligating moiety.
K J, Lee, D H, Kim
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Tyrosine fluorescence as a measure of denaturation in thermolysin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
The heat and guanidine hydrochloride denaturation of thermolysin has been followed by fluorescence techniques. The native enzyme has a single emission peak which is decreased in intensity and which splits into two clearly resolved peaks upon denaturation.
S M, Khan, D W, Darnall, E R, Birnbaum
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Role of calcium in the thermal stability of thermolysin

Biochemistry, 1976
The effect of calcium ion on the thermal stability of thermolysin has been investigated. The native protein undergoes an irreversible structural change and autolysis at high temperature. Analysis of the calcium ion dependence of the apparent melting temperature observed spectroscopically gives an apparent deltaH of -x (130 kcal/mol) where x is either 1
F W, Dahlquist, J W, Long, W L, Bigbee
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Inhibition of thermolysin by N-carboxymethyl dipeptides

Biochemical and Biophysical Research Communications, 1981
Abstract A design principle effective for generating inhibitors of angiotensin converting enzyme has been successfully extended to inhibitors of another Zn ++ endopeptidase, thermolysin. Hence, N-(1-carboxy-3-phenylpropyl)LeuTrp is found to be a potent inhibitor of thermolysin, K i ∼ 5 × 10 −8 M.
A L, Maycock, D M, DeSousa, L G, Payne, J, ten Broeke, M T, Wu, A A, Patchett   +5 more
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