MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data-Reference-Cited by-同舟云学术

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MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data

Published:2015-07-29 Issue:1 Volume:63 Page:85-95
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Mantsyzov Alexey B.,Shen Yang,Lee Jung Ho,Hummer Gerhard,Bax Ad

Funder

National Institutes of Health

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-015-9971-2.pdf

Reference51 articles.

1. Baldwin RL, Rose GD (1999) Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 24:26–33

2. Ball KA, Phillips AH, Nerenberg PS, Fawzi NL, Wemmer DE, Head-Gordon T (2011) Homogeneous and heterogeneous tertiary structure ensembles of amyloid-beta peptides. Biochemistry 50:7612–7628

3. Berjanskii MV, Wishart DS (2005) A simple method to predict protein flexibility using secondary chemical shifts. J Am Chem Soc 127:14970–14971

4. Bernado P, Mylonas E, Petoukhov MV, Blackledge M, Svergun DI (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 129:5656–5664

5. Bertoncini CW, Rasia RM, Lamberto GR, Binolfi A, Zweckstetter M, Griesinger C, Fernandez CO (2007) Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation. J Mol Biol 372:708–722

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