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The rate of equine liver alcohol dehydrogenase denaturation by urea dependence on temperature and denaturant concentration

โœ Scribed by Margherita Gonnelli; Giovanni Battista Strambini


Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
559 KB
Volume
24
Category
Article
ISSN
0301-4622

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Like most dehydrogenases, with horse liver alcohol dehydrogenase (LADH), a bulky amino acid residue (Val 203) is positioned at the face of NAD + distal to substrate alcohol in order to restrict the separation of reactants and to control the stereochemistry. Molecular dynamics simulations of native (