Comparative studies on trifluoroethanol (TFE) state of a thermophilic α-amylase and its mesophilic counterpart: limited proteolysis, conformational analysis, aggregation and reactivation of the enzymes-Reference-Cited by-同舟云学术

Comparative studies on trifluoroethanol (TFE) state of a thermophilic α-amylase and its mesophilic counterpart: limited proteolysis, conformational analysis, aggregation and reactivation of the enzymes

Published:2004-06 Issue:3 Volume:34 Page:173-179
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Asghari S.Mohsen,Khajeh Khosro,Ranjbar Bijan,Sajedi Reza H,Naderi-Manesh Hossein

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference56 articles.

1. Pulsed H/D-exchange studies of folding intermediates

2. Is the molten globule a third phase of proteins?

3. Native-like β-structure in a Trifluoroethanol-induced Partially Folded State of the All-β-sheet Protein Tendamistat

4. Unfolded proteins, compact states and molten globules

5. pH and Temperature-Induced Molten Globule-Like Denatured States of Equinatoxin II: A Study by UV-Melting, DSC, Far- and Near-UV CD Spectroscopy, and ANS Fluorescence

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