Related ArticlesNMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
J Phys Chem B. 2012 Dec 13;116(49):14207-15
Authors: Sonti R, Rai R, Ragothama S, Balaram P
Abstract
Cross strand aromatic interactions between a facing pair of phenylalanine residues in antiparallel ?-sheet structures have been probed using two structurally defined model peptides. The octapeptide Boc-LFV(D)P(L)PLFV-OMe (peptide 1) favors the ?-hairpin conformation nucleated by the type II' ?-turn formed by the (D)Pro-(L)Pro segment, placing Phe2 and Phe7 side chains in proximity. Two centrally positioned (D)Pro-(L)Pro segments facilitate the three stranded ?-sheet formation in the 14 residue peptide Boc-LFV(D)P(L)PLFVA(D)P(L)PLFV-OMe (peptide 2) in which the Phe2/Phe7 orientations are similar to that in the octapeptide. The anticipated folded conformations of peptides 1 and 2 are established by the delineation of intramolecularly hydrogen bonded NH groups and by the observation of specific cross strand NOEs. The observation of ring current shifted aromatic protons is a diagnostic of close approach of the Phe2 and Phe7 side chains. Specific assignment of aromatic proton resonances using HSQC and HSQC-TOCSY methods allow an analysis of interproton NOEs between the spatially proximate aromatic rings. This approach facilitates specific assignments in systems containing multiple aromatic rings in spectra at natural abundance. Evidence is presented for a dynamic process which invokes a correlated conformational change about the C(?)-C(?)(?(1)) bond for the pair of interacting Phe residues. NMR results suggest that aromatic ring orientations observed in crystals are maintained in solution. Anomalous temperature dependence of ring current induced proton chemical shifts suggests that solvophobic effects may facilitate aromatic ring clustering in apolar solvents.
[NMR paper] pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
Related Articles pH-Dependent Conformation, Dynamics, and Aromatic Interaction of*the*Gating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR.
Biophys J. 2013 Apr 16;104(8):1698-708
Authors: Williams JK, Zhang Y, Schmidt-Rohr K, Hong M
Abstract
The M2 protein of the influenza virus conducts protons into the virion under external acidic pH. The proton selectivity of...
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04-23-2013 08:37 PM
NMR for a 30-residue peptide
Dear all,
Is that possible to do structure determination of a 30-residue peptide
using 500 MHz NMR?
I have a 30-residue linear peptide with three Gly and two AHx
(aminohexanoic acid) groups at the center of the peptide. I read some
papers from people who use 500 MHz NMR to determine the structure of
up to 20-residue peptides, but not a 30-residue peptide.
bimo
NMR Questions and Answers
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03-06-2013 12:35 AM
Alternative SAIL-Trp for robust aromatic signal assignment and determination of the Ď?2 conformation by intra-residue NOEs
Alternative SAIL-Trp for robust aromatic signal assignment and determination of the Ď?2 conformation by intra-residue NOEs
Abstract Tryptophan (Trp) residues are frequently found in the hydrophobic cores of proteins, and therefore, their side-chain conformations, especially the precise locations of the bulky indole rings, are critical for determining structures by NMR. However, when analyzing -proteins, the observation and assignment of the ring signals are often hampered by excessive overlaps and tight spin couplings. These difficulties have been greatly alleviated by using...
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09-27-2011 07:04 AM
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Protein Expr Purif. 2011 May 27;
Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
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06-07-2011 11:05 AM
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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03-08-2011 01:40 PM
[NMR paper] Design, NMR characterization and activity of a 21-residue peptide fragment of bacteri
Design, NMR characterization and activity of a 21-residue peptide fragment of bacteriocin AS-48 containing its putative membrane interacting region.
Related Articles Design, NMR characterization and activity of a 21-residue peptide fragment of bacteriocin AS-48 containing its putative membrane interacting region.
J Pept Sci. 2005 Jan;11(1):29-36
Authors: Jiménez MA, Barrachi-Saccilotto AC, Valdivia E, Maqueda M, Rico M
Bacteriocin AS-48 is a 70-residue cyclic polypeptide from Enterococcus faecalis that shows a broad antimicrobial spectrum...
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11-24-2010 11:14 PM
[NMR paper] Structural characterization of a 39-residue synthetic peptide containing the two zinc
Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
FEBS Lett. 1991 Nov 4;292(1-2):25-30
Authors: Omichinski JG, Clore GM, Sakaguchi K, Appella E,...
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08-21-2010 11:12 PM
[NMR paper] Structural characterization of a 39-residue synthetic peptide containing the two zinc
Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
FEBS Lett. 1991 Nov 4;292(1-2):25-30
Authors: Omichinski JG, Clore GM, Sakaguchi K, Appella E,...
NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
Linear Mode
