Structural changes of α-chymotrypsin in reverse micelles of AOT studied by steady state and transient state fluorescence spectroscopy
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry
Reference9 articles.
1. Resolved Fluorescence of the Two Tryptophan Residues in Horse Apomyoglobin
2. Comparison of the dynamic structure of alpha-chymotrypsin in aqueous solution and in reversed micelles by fluorescent active-site probing
3. The Location of Tryptophan, N-acetyltryptophan and α-Chymotrypsin in Reverse Micelles of AOT: A Fluorescence Study¶
4. Time-Resolved Distance Determination by Tryptophan Fluorescence Quenching: Probing Intermediates in Membrane Protein Folding
5. [19] Activity and conformation of enzymes in reverse micellar solutions
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3. Nanoenvironmental effect in AOT reverse micelles on the triplet excited state properties of flavins and quenching by molecular oxygen;Journal of Physical Organic Chemistry;2016-05-19
4. Extraction and purification of laccase by employing a novel rhamnolipid reversed micellar system;Process Biochemistry;2012-05
5. Cationic Reverse Micelles Create Water with Super Hydrogen-Bond-Donor Capacity for Enzymatic Catalysis: Hydrolysis of 2-Naphthyl Acetate by α-Chymotrypsin;Chemistry - A European Journal;2010-06-22
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