Analysis of Internally Restricted Correlated Rotations in Peptides and Proteins Using 13C and 15N NMR Relaxation Data-Reference-Cited by-同舟云学术

Analysis of Internally Restricted Correlated Rotations in Peptides and Proteins Using 13C and 15N NMR Relaxation Data

Published:1996-01-01 Issue:20 Volume:100 Page:8378-8388
ISSN:0022-3654
Container-title:The Journal of Physical Chemistry
language:en
Short-container-title:J. Phys. Chem.

Author:

Daragan Vladimir A.¹,Mayo Kevin H.¹

Affiliation:

1. Department of Biochemistry, Biomedical Engineering Center, University of Minnesota Health Sciences Center, 420 Delaware Street, S.E., Minneapolis, Minnesota 55455

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,General Engineering

Link

https://pubs.acs.org/doi/pdf/10.1021/jp9531927

Reference20 articles.

1. NMR of Proteins; Clore, G. M., Gronenborn, A. M., Eds; CRC Press: Boca Raton, FL, 1993.

2. Heteronuclear Dipolar Cross-Correlated Cross Relaxation for the Investigation of Side-Chain Motions

3. 13C-Coupled Relaxation Studies of a Leucine Zipper Peptide Using Polarization-Transfer Pulse Sequences

4. Using the Model-Free Approach to Interpret 13C NMR Multiplet Relaxation Data from Peptides and Proteins

5. Spin-lattice relaxation of coupled nuclear spins with applications to molecular motion in liquids

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