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Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability

Protein thermal dynamics was evaluated by neutron scattering for halophilic malate dehydrogenase from Haloarcula marismortui (HmMalDH) and BSA under different solvent conditions. As a measure of thermal stability in each case, loss of secondary structure temperatures were determined by CD. HmMalDH r...

Πλήρης περιγραφή

Αποθηκεύτηκε σε:
Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς: Tehei, Moeava, Madern, Dominique, Pfister, Claude, Zaccai, Giuseppe
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: The National Academy of Sciences 2001
Θέματα:
Διαθέσιμο Online:https://ncbi.nlm.nih.gov/pmc/articles/PMC64686/
https://ncbi.nlm.nih.gov/pubmed/11734642
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.251537298
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