Literature DB >> 17541576

Magnetic resonance in the solid state: applications to protein folding, amyloid fibrils and membrane proteins.

Marc Baldus1.   

Abstract

Solid-state nuclear magnetic resonance (ssNMR) represents a spectroscopic method to study non-crystalline molecules at atomic resolution. Advancements in spectroscopy and biochemistry provide increasing possibilities to study structure and dynamics of complex biomolecular systems by ssNMR. Here, methodological aspects and applications in the context of protein folding and aggregation are discussed. In addition, studies involving membrane proteins are considered.

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Year:  2007        PMID: 17541576     DOI: 10.1007/s00249-007-0174-y

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN: 0175-7571            Impact factor:   1.733


  99 in total

Review 1.  Solid-state NMR spectroscopy applied to membrane proteins.

Authors:  H J de Groot
Journal:  Curr Opin Struct Biol       Date:  2000-10       Impact factor: 6.809

2.  High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.

Authors:  Christopher P Jaroniec; Cait E MacPhee; Vikram S Bajaj; Michael T McMahon; Christopher M Dobson; Robert G Griffin
Journal:  Proc Natl Acad Sci U S A       Date:  2004-01-08       Impact factor: 11.205

Review 3.  Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR.

Authors:  Mei Hong
Journal:  Structure       Date:  2006-12       Impact factor: 5.006

Review 4.  Dipolar recoupling in MAS spectra of biological solids.

Authors:  R G Griffin
Journal:  Nat Struct Biol       Date:  1998-07

5.  Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

Authors:  M Sunde; L C Serpell; M Bartlam; P E Fraser; M B Pepys; C C Blake
Journal:  J Mol Biol       Date:  1997-10-31       Impact factor: 5.469

6.  Protein folding monitored at individual residues during a two-dimensional NMR experiment.

Authors:  J Balbach; V Forge; W S Lau; N A van Nuland; K Brew; C M Dobson
Journal:  Science       Date:  1996-11-15       Impact factor: 47.728

Review 7.  High-resolution NMR of biological solids.

Authors:  L M McDowell; J Schaefer
Journal:  Curr Opin Struct Biol       Date:  1996-10       Impact factor: 6.809

8.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology.

Authors:  G Cornilescu; F Delaglio; A Bax
Journal:  J Biomol NMR       Date:  1999-03       Impact factor: 2.835

9.  Correlation of structural elements and infectivity of the HET-s prion.

Authors:  Christiane Ritter; Marie-Lise Maddelein; Ansgar B Siemer; Thorsten Lührs; Matthias Ernst; Beat H Meier; Sven J Saupe; Roland Riek
Journal:  Nature       Date:  2005-06-09       Impact factor: 49.962

10.  General structural motifs of amyloid protofilaments.

Authors:  Neil Ferguson; Johanna Becker; Henning Tidow; Sandra Tremmel; Timothy D Sharpe; Gerd Krause; Jeremy Flinders; Miriana Petrovich; John Berriman; Hartmut Oschkinat; Alan R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  2006-10-23       Impact factor: 11.205

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  8 in total

1.  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

2.  Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes.

Authors:  Lei Shi; Alessandro Cembran; Jiali Gao; Gianluigi Veglia
Journal:  Biophys J       Date:  2009-05-06       Impact factor: 4.033

3.  Study of Amyloids Using Yeast.

Authors:  Reed B Wickner; Dmitry Kryndushkin; Frank Shewmaker; Ryan McGlinchey; Herman K Edskes
Journal:  Methods Mol Biol       Date:  2018

4.  Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements.

Authors:  Patrick C A van der Wel; Matthew T Eddy; Ramesh Ramachandran; Robert G Griffin
Journal:  Chemphyschem       Date:  2009-07-13       Impact factor: 3.102

5.  Secondary structural analysis of proteins based on (13)C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database.

Authors:  Keisuke Ikeda; Ayako Egawa; Toshimichi Fujiwara
Journal:  J Biomol NMR       Date:  2012-12-29       Impact factor: 2.835

6.  Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.

Authors:  Raffaello Verardi; Lei Shi; Nathaniel J Traaseth; Naomi Walsh; Gianluigi Veglia
Journal:  Proc Natl Acad Sci U S A       Date:  2011-05-16       Impact factor: 11.205

7.  Study of amyloids using yeast.

Authors:  Reed B Wickner; Dmitry Kryndushkin; Frank Shewmaker; Ryan McGlinchey; Herman K Edskes
Journal:  Methods Mol Biol       Date:  2012

8.  Cu(II) binding to various forms of amyloid-β peptides. Are they friends or foes?

Authors:  Valentina Borghesani; Bruno Alies; Christelle Hureau
Journal:  Eur J Inorg Chem       Date:  2018-01-10       Impact factor: 2.524

  8 in total

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