Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor: Multisite Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling-Reference-Cited by-同舟云学术

Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor: Multisite Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling

Published:2003-10-29 Issue:47 Volume:125 Page:14324-14335
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Grey Michael J.¹,Wang Chunyu¹,Palmer Arthur G.¹

Affiliation:

1. Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, New York 10032

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0367389

Reference82 articles.

1. Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR Spectroscopy

2. Using Amide 1H and 15N Transverse Relaxation To Detect Millisecond Time-Scale Motions in Perdeuterated Proteins: Application to HIV-1 Protease

3. A Relaxation-Compensated Carr−Purcell−Meiboom−Gill Sequence for Characterizing Chemical Exchange by NMR Spectroscopy

4. Transverse 13C Relaxation of CHD2 Methyl Isotopmers To Detect Slow Conformational Changes of Protein Side Chains

5. The Static Magnetic Field Dependence of Chemical Exchange Linebroadening Defines the NMR Chemical Shift Time Scale

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