Literature DB >> 14568611

TROSY in NMR studies of the structure and function of large biological macromolecules.

César Fernández1, Gerhard Wider.   

Abstract

Transverse relaxation-optimized spectroscopy (TROSY), in combination with various isotope-labeling techniques, has opened avenues to study biomolecules with molecular masses of up to 1000000Da by solution NMR. Important recent applications of TROSY include the structure determination of membrane proteins in detergent micelles, structural and functional studies of large proteins in both monomeric form and macromolecular complexes, and investigations of intermolecular interactions in large complexes. TROSY improves the measurement of residual dipolar couplings and the detection of scalar couplings across hydrogen bonds - techniques that promise to further enhance the determination of solution structures of large proteins and oligonucleotides.

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Year:  2003        PMID: 14568611     DOI: 10.1016/j.sbi.2003.09.009

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  39 in total

1.  Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle.

Authors:  Alexandra Choutko; Alice Glättli; César Fernández; Christian Hilty; Kurt Wüthrich; Wilfred F van Gunsteren
Journal:  Eur Biophys J       Date:  2010-10-05       Impact factor: 1.733

2.  Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent.

Authors:  Brett M Kroncke; Linda Columbus
Journal:  Protein Sci       Date:  2012-03-02       Impact factor: 6.725

Review 3.  Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.

Authors:  Hazime Saitô; Isao Ando; Ayyalusamy Ramamoorthy
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2010-05-07       Impact factor: 9.795

4.  Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.

Authors:  Hak Jun Kim; Stanley C Howell; Wade D Van Horn; Young Ho Jeon; Charles R Sanders
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2009-11-01       Impact factor: 9.795

5.  Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

Authors:  Reto Horst; Eric B Bertelsen; Jocelyne Fiaux; Gerhard Wider; Arthur L Horwich; Kurt Wüthrich
Journal:  Proc Natl Acad Sci U S A       Date:  2005-08-22       Impact factor: 11.205

Review 6.  First glimpses of a chaperonin-bound folding intermediate.

Authors:  Joanna F Swain; Lila M Gierasch
Journal:  Proc Natl Acad Sci U S A       Date:  2005-09-19       Impact factor: 11.205

7.  When monomers are preferred: a strategy for the identification and disruption of weakly oligomerized proteins.

Authors:  Yufeng Tong; David Hughes; Lisa Placanica; Matthias Buck
Journal:  Structure       Date:  2005-01       Impact factor: 5.006

8.  13C- 13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin.

Authors:  Manolis Matzapetakis; Paola Turano; Elizabeth C Theil; Ivano Bertini
Journal:  J Biomol NMR       Date:  2007-06-07       Impact factor: 2.835

9.  Dynamic inter-subunit interactions in thermophilic F(1)-ATPase subcomplexes studied by cross-correlated relaxation-enhanced polarization transfer NMR.

Authors:  Masumi Kobayashi; Hiromasa Yagi; Toshio Yamazaki; Masasuke Yoshida; Hideo Akutsu
Journal:  J Biomol NMR       Date:  2008-01-05       Impact factor: 2.835

10.  SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.

Authors:  Lucio Ferella; Claudio Luchinat; Enrico Ravera; Antonio Rosato
Journal:  J Biomol NMR       Date:  2013-11-17       Impact factor: 2.835

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