Stability of protease in organic solvent: Structural identification by solid-state NMR of lyophilized papain before and after 1-propanol treatment and the corresponding enzymatic activities-Reference-Cited by-同舟云学术

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Stability of protease in organic solvent: Structural identification by solid-state NMR of lyophilized papain before and after 1-propanol treatment and the corresponding enzymatic activities

Published:2006 Issue:5 Volume:93 Page:928-933
ISSN:0006-3592
Container-title:Biotechnology and Bioengineering
language:en
Short-container-title:Biotechnol. Bioeng.

Author:

Matsubara Teruhiko,Fujita Risa,Sugiyama Shigeru,Kawashiro Katsuhiro

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Reference30 articles.

1. Ab Initio Study of 13Cα Chemical Shift Anisotropy Tensors in Peptides

2. Solid-state NMR assessment of enzyme active center structure under nonaqueous conditions.

3. Relationship between conformational stability and lyophilization-induced structural changes in chymotrypsin

4. Assessing the Structural Integrity of a Lyophilized Protein in Organic Solvents

5. Protein Structure in the Lyophilized State: A Hydrogen Isotope Exchange/NMR Study with Bovine Pancreatic Trypsin Inhibitor

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2. Current Electrospray Mass Spectrometry: An Overview. Part B. Analyte Charging;Encyclopedia of Analytical Chemistry;2015-01-22

3. A molecular perspective on nonaqueous biocatalysis: contributions from simulation studies;Physical Chemistry Chemical Physics;2013

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