Literature DB >> 20483310

Mapping the conformational mobility of multidomain proteins.

Martin Blackledge.   

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Year:  2010        PMID: 20483310      PMCID: PMC2872266          DOI: 10.1016/j.bpj.2010.03.005

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


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  6 in total

1.  General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation.

Authors:  Jeanine J Prompers; Rafael Brüschweiler
Journal:  J Am Chem Soc       Date:  2002-04-24       Impact factor: 15.419

Review 2.  NMR studies of modular protein structures and their interactions.

Authors:  Andrew R Pickford; Iain D Campbell
Journal:  Chem Rev       Date:  2004-08       Impact factor: 60.622

3.  Structural characterization of flexible proteins using small-angle X-ray scattering.

Authors:  Pau Bernadó; Efstratios Mylonas; Maxim V Petoukhov; Martin Blackledge; Dmitri I Svergun
Journal:  J Am Chem Soc       Date:  2007-04-06       Impact factor: 15.419

Review 4.  Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.

Authors:  Malene Ringkjøbing Jensen; Phineus R L Markwick; Sebastian Meier; Christian Griesinger; Markus Zweckstetter; Stephan Grzesiek; Pau Bernadó; Martin Blackledge
Journal:  Structure       Date:  2009-09-09       Impact factor: 5.006

5.  Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.

Authors:  Pau Bernadó; Kristofer Modig; Przemysław Grela; Dmitri I Svergun; Marek Tchorzewski; Miquel Pons; Mikael Akke
Journal:  Biophys J       Date:  2010-05-19       Impact factor: 4.033

Review 6.  Intrinsic disorder and functional proteomics.

Authors:  Predrag Radivojac; Lilia M Iakoucheva; Christopher J Oldfield; Zoran Obradovic; Vladimir N Uversky; A Keith Dunker
Journal:  Biophys J       Date:  2006-12-08       Impact factor: 4.033

  6 in total
  1 in total

1.  Flexibility in the Periplasmic Domain of BamA Is Important for Function.

Authors:  Lisa R Warner; Petia Z Gatzeva-Topalova; Pamela A Doerner; Arthur Pardi; Marcelo C Sousa
Journal:  Structure       Date:  2016-12-15       Impact factor: 5.006

  1 in total

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