Related ArticlesProbing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions.
J Magn Reson. 1999 Dec;141(2):335-9
Authors: Gröbner G, Glaubitz C, Watts A
A simple but efficient (13)C MAS NMR method is presented for the determination of the location of embedded molecules such as peptides relative to biological membrane surfaces by exploiting the interaction with paramagnetic lanthanide ions. Using various aqueous Dy(3+) concentrations a distance-dependent differential paramagnetic quenching of NMR lipid resonance intensities for specific carbon sites was observed, with residues at the bilayer surface quenched effectively and hydrophobic sites unaffected by Dy(3+). Tested on the membrane-embedded 50 residue long M13 coat protein, (13)C labeled at its Val-29 and Val-31 residues, no paramagnetic quenching was observed for the peptide resonances by Dy(3+), suggesting that Val-29 and Val-31 are not in close proximity to the bilayer interface, but buried deeply inside the hydrophobic region of the lipid bilayer.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
J Phys Chem B. 2011 Aug 1;
Authors: Su Y, Hong M
A challenge in the application of solid-state NMR spectroscopy to membrane proteins and peptides is the relatively broad linewidths compared to solution NMR spectra. To understand the linewidth contributions to membrane protein spectra, we have measured the inhomogeneous and homogeneous...
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08-03-2011 12:00 PM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
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02-24-2011 11:04 AM
[NMR paper] Probing membrane protein orientation and structure using fast magic-angle-spinning so
Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
Related Articles Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
J Biomol NMR. 2004 Nov;30(3):253-65
Authors: Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DT, Angerstein B, Luca S, Koert U, Killian JA, Baldus M
One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides...
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11-24-2010 10:03 PM
[NMR paper] The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics de
The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy.
Related Articles The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy.
Biochim Biophys Acta. 2004 Nov 17;1667(1):67-81
Authors: Morris KF, Gao X, Wong TC
The wild-type (wt) N-terminal 23-residue fusion peptide (FP) of the human immunodeficiency virus (HIV) fusion protein gp41 and its V2E mutant have been studied by nuclear magnetic resonance (NMR) spectroscopy in...
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[NMR paper] Structural and orientational information of the membrane embedded M13 coat protein by
Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Related Articles Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Biochim Biophys Acta. 2000 Jan 15;1463(1):151-61
Authors: Glaubitz C, Gröbner G, Watts A
Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational...
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Related Articles Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Biochim Biophys Acta. 2010 Aug 15;
Authors: Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is...
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Solid State NMR of membrane peptides and proteins
Solid State NMR of membrane peptides and proteins
Lecture notes on "Solid State NMR of membrane peptides and proteins" by Dr. SK Straus from Univ. of British Columbia
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Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS
Linear Mode
