Internal protein dynamics on ps to μs timescales as studied by multi-frequency 15N solid-state NMR relaxation-Reference-Cited by-同舟云学术

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Internal protein dynamics on ps to μs timescales as studied by multi-frequency 15N solid-state NMR relaxation

Published:2013-09-19 Issue:3 Volume:57 Page:219-235
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Zinkevich Tatiana,Chevelkov Veniamin,Reif Bernd,Saalwächter Kay,Krushelnitsky Alexey

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-013-9782-2.pdf

Reference68 articles.

1. Abdullah A, Deris S, Anwar S, Arjunan SNV (2013) An evolutionary firefly algorithm for the estimation of nonlinear biological model parameters. PLoS ONE 8:e56310

2. Agarwal V, Xue Y, Reif B, Skrynnikov NR (2008) Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed. J Am Chem Soc 130:16611–16621

3. Akaike H (1974) Stochastic theory of minimal realization. IEEE Trans Automat Contr 19:667–674

4. Akasaka K (1983) Spin–spin and spin-lattice contributions to the rotating frame relaxation of 13C in l-alanine. J Chem Phys 78:3567–3572

5. Baldus M (2002) Correlation experiments for assignment and structure elucidation of immobilized polypeptides under magic angle spinning. Prog Nucl Magn Reson Spectrosc 41:1–47

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