Literature DB >> 19647984

Structure elucidation of membrane-associated peptides and proteins in oriented bilayers by solid-state NMR spectroscopy.

Akira Naito1.   

Abstract

Solid-state NMR using magnetically oriented bilayer systems provides useful information on the structure and orientation of peptides and proteins bound to lipid bilayers. The ordering of the lipid bilayer along the magnetic field can be achieved in two ways. First, lipid can be macroscopically oriented by pressing lipid-water dispersion between flat glass plates, which is called a mechanically aligned system. Second, lipid molecules themselves can be aligned spontaneously in the magnetic field because of their diamagnetic anisotropy by forming bicelles or magnetically oriented vesicle systems. Structure and orientation of the membrane-associated peptides and proteins can be achieved by analyzing structural constraints obtained from anisotropic chemical shift interactions such as chemical shift oscillation or nuclear dipolar interactions such as dipolar wave and a combination of them such as PISA wheel. Detailed structure elucidation of various kinds of membrane peptides and proteins in such oriented bilayers is presented.

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Year:  2009        PMID: 19647984     DOI: 10.1016/j.ssnmr.2009.06.008

Source DB:  PubMed          Journal:  Solid State Nucl Magn Reson        ISSN: 0926-2040            Impact factor:   2.293


  16 in total

1.  High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.

Authors:  Meaghan E Ward; Shenlin Wang; Sridevi Krishnamurthy; Howard Hutchins; Michael Fey; Leonid S Brown; Vladimir Ladizhansky
Journal:  J Biomol NMR       Date:  2013-12-13       Impact factor: 2.835

Review 2.  Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.

Authors:  Akira Naito; Nobuaki Matsumori; Ayyalusamy Ramamoorthy
Journal:  Biochim Biophys Acta Gen Subj       Date:  2017-06-06       Impact factor: 3.770

3.  The development of solid-state NMR of membrane proteins.

Authors:  Stanley J Opella
Journal:  Biomed Spectrosc Imaging       Date:  2014

4.  Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.

Authors:  Nathaniel J Traaseth; Gianluigi Veglia
Journal:  J Magn Reson       Date:  2011-03-17       Impact factor: 2.229

5.  Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.

Authors:  T Gopinath; Gianluigi Veglia
Journal:  Chem Phys Lett       Date:  2010-07-09       Impact factor: 2.328

6.  Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.

Authors:  Shuichi Toraya; Namsrai Javkhlantugs; Daisuke Mishima; Katsuyuki Nishimura; Kazuyoshi Ueda; Akira Naito
Journal:  Biophys J       Date:  2010-11-17       Impact factor: 4.033

7.  A proton spin diffusion based solid-state NMR approach for structural studies on aligned samples.

Authors:  Jiadi Xu; Pieter E S Smith; Ronald Soong; Ayyalusamy Ramamoorthy
Journal:  J Phys Chem B       Date:  2011-04-05       Impact factor: 2.991

8.  On the performance of spin diffusion NMR techniques in oriented solids: prospects for resonance assignments and distance measurements from separated local field experiments.

Authors:  Nathaniel J Traaseth; T Gopinath; Gianluigi Veglia
Journal:  J Phys Chem B       Date:  2010-11-04       Impact factor: 2.991

Review 9.  Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.

Authors:  Raffaello Verardi; Nathaniel J Traaseth; Larry R Masterson; Vitaly V Vostrikov; Gianluigi Veglia
Journal:  Adv Exp Med Biol       Date:  2012       Impact factor: 2.622

Review 10.  Spatial reorientation experiments for NMR of solids and partially oriented liquids.

Authors:  Rachel W Martin; John E Kelly; Kelsey A Collier
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2015-10-23       Impact factor: 9.795

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