Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data-Reference-Cited by-同舟云学术

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Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data

Published:2016-01-28 Issue:9 Volume:55 Page:3117-3119
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Gu Yina¹,Hansen Alexandar L.²,Peng Yu¹,Brüschweiler Rafael¹²³

Affiliation:

1. Department of Chemistry and Biochemistry The Ohio State University 100 West 18th Avenue Columbus OH 43210 USA

2. Campus Chemical Instrument Center The Ohio State University 460 W. 12th Avenue Columbus OH 43210 USA

3. Department of Biological Chemistry and Pharmacology The Ohio State University 1645 Neil Avenue Columbus OH 43210 USA

Funder

National Science Foundation

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201511711

Reference46 articles.

1.

2. Measurement of Proton Chemical Shifts in Invisible States of Slowly Exchanging Protein Systems by Chemical Exchange Saturation Transfer

3. A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding

4. Studying “Invisible” Excited Protein States in Slow Exchange with a Major State Conformation

5. Characterizing Slow Chemical Exchange in Nucleic Acids by Carbon CEST and Low Spin-Lock Field R1ρ NMR Spectroscopy

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3. Protein Backbone and Side-chain 15N Spin Relaxation Techniques to Study Biomacromolecular Interactions;NMR Spectroscopy for Probing Functional Dynamics at Biological Interfaces;2022-08-17

4. NOAH-(¹⁵N/¹³C)-CEST NMR supersequence for dynamics studies of biomolecules;Chemical Communications;2022

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