Literature DB >> 15808228

NMR experiments on aligned samples of membrane proteins.

A A De Angelis1, D H Jones, C V Grant, S H Park, M F Mesleh, S J Opella.   

Abstract

NMR methods can be used to determine the structures of membrane proteins. Lipids can be chosen so that protein-containing micelles, bicelles, or bilayers are available as samples. All three types of samples can be aligned weakly or strongly, depending on their rotational correlation time. Solution NMR methods can be used with weakly aligned micelle and small bicelle samples. Solid-state NMR methods can be used with mechanically aligned bilayer and magnetically aligned bicelle samples.

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Year:  2005        PMID: 15808228     DOI: 10.1016/S0076-6879(05)94014-7

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  30 in total

1.  Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly.

Authors:  Sang Ho Park; Francesca M Marassi; David Black; Stanley J Opella
Journal:  Biophys J       Date:  2010-09-08       Impact factor: 4.033

2.  Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.

Authors:  Martin Gustavsson; Nathaniel J Traaseth; Gianluigi Veglia
Journal:  Biochim Biophys Acta       Date:  2011-08-03

3.  Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy.

Authors:  Anna A De Angelis; Stanley C Howell; Alexander A Nevzorov; Stanley J Opella
Journal:  J Am Chem Soc       Date:  2006-09-20       Impact factor: 15.419

4.  An efficient (1)H/(31)P double-resonance solid-state NMR probe that utilizes a scroll coil.

Authors:  Christopher V Grant; Siu-Ling Sit; Anna A De Angelis; Kelli S Khuong; Chin H Wu; Leigh A Plesniak; Stanley J Opella
Journal:  J Magn Reson       Date:  2007-08-06       Impact factor: 2.229

5.  High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument.

Authors:  Alfred G Redfield
Journal:  J Biomol NMR       Date:  2011-12-27       Impact factor: 2.835

6.  Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.

Authors:  Andrew K Lewis; Zachary M James; Jesse E McCaffrey; Anthony R Braun; Christine B Karim; David D Thomas; Jonathan N Sachs
Journal:  Biophys J       Date:  2014-03-18       Impact factor: 4.033

7.  Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.

Authors:  Radhakrishnan Mahalakshmi; Francesca M Marassi
Journal:  Biochemistry       Date:  2008-06-24       Impact factor: 3.162

8.  Amphipathic antimicrobial piscidin in magnetically aligned lipid bilayers.

Authors:  Anna A De Angelis; Christopher V Grant; Matthew K Baxter; Jason A McGavin; Stanley J Opella; Myriam L Cotten
Journal:  Biophys J       Date:  2011-09-07       Impact factor: 4.033

9.  Sensitivity enhancement of separated local field experiments: application to membrane proteins.

Authors:  T Gopinath; Raffaello Verardi; Nathaniel J Traaseth; Gianluigi Veglia
Journal:  J Phys Chem B       Date:  2010-04-22       Impact factor: 2.991

Review 10.  Probes for high field solid-state NMR of lossy biological samples.

Authors:  Christopher V Grant; Chin H Wu; Stanley J Opella
Journal:  J Magn Reson       Date:  2010-03-31       Impact factor: 2.229

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