Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy-Reference-Cited by-同舟云学术

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Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy

Published:1997-06 Issue:6 Volume:4 Page:443-449
ISSN:1072-8368
Container-title:Nature Structural Biology
language:
Short-container-title:Nat Struct Mol Biol

Author:

Tjandra Nico,Garrett Daniel S.,Gronenborn Angela M.,Bax Ad,Clore G. Marius

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Biochemistry,Structural Biology

Reference30 articles.

1. Wüthrich, K. NMR of Proteins. (Wiley, New York, 1986).

2. Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance Spectroscop

3. Structure and distribution of modules in extracellular proteins

4. Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance

5. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity

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