Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White Lysozyme-Reference-Cited by-同舟云学术

Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White Lysozyme

Published:1995-03-28 Issue:12 Volume:34 Page:4041-4055
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Buck Matthias,Boyd Jonathan,Redfield Christina,MacKenzie Donald A.,Jeenes David J.,Archer David B.,Dobson Christopher M.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00012a023

Reference81 articles.

1. Crystallographic studies of the dynamic properties of lysozyme

2. Primary structure effects on peptide group hydrogen exchange

3. Hydrogen bonding in globular proteins

4. Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible

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