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A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes.

The thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase made of parts from an extreme thermophile, Thermus thermophilus, and a mesophile, Bacillus subtilis, enzymes was studied by CD spectrophotometry and differential scanning calorimetry (DSC). The enzyme is a homodimer with a s...

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Bibliografiske detaljer
Main Authors: Hayashi-Iwasaki, Y., Numata, K., Yamagishi, A., Yutani, K., Sakurai, M., Tanaka, N., Oshima, T.
Format: Artigo
Sprog:Inglês
Udgivet: Cold Spring Harbor Laboratory Press 1996
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143370/
https://ncbi.nlm.nih.gov/pubmed/8868488
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