Related ArticlesStructure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR.
J Am Chem Soc. 2004 Apr 7;126(13):4199-210
Authors: Yao XL, Hong M
Elastin is an extracellular-matrix protein that imparts elasticity to tissues. We have used solid-state NMR to determine a number of distances and torsion angles in an elastin-mimetic peptide, (VPGVG)3, to understand the structural basis of elasticity. C-H and C-N distances between the V6 carbonyl and the V9 amide segment were measured using 13C-15N and 13C-1H rotational-echo double-resonance experiments. The results indicate the coexistence of two types of intramolecular distances: a third of the molecules have short C-H and C-N distances of 3.3 +/- 0.2 and 4.3 +/- 0.2 A, respectively, while the rest have longer distances of about 7 A. Complementing the distance constraints, we measured the (phi, psi ) torsion angles of the central pentameric unit using dipolar correlation NMR. The -angles of P7 and G8 are predominantly ~150, thus restricting the majority of the peptide to be extended. Combining all torsion angles measured for the five residues, the G8 C chemical shift, and the V6-V9 distances, we obtained a bimodal structure distribution for the PG residues in VPGVG. The minor form is a compact structure with a V6-V9 C=O-HN hydrogen bond and can be either a type II -turn or a previously unidentified turn with Pro (phi = -70, psi= 20 +/- 20) and Gly ( phi= -100 +/- 20, psi = -20 +/- 20). The major form is an extended and distorted beta-strand without a V6-V9 hydrogen bond and differs from the ideal parallel and antiparallel beta-strands. The other three residues in the VPGVG unit mainly adopt antiparallel beta-sheet torsion angles. Since (VPGVG)3 has the same 13C and 15N isotropic and anisotropic chemical shifts as the elastin-mimetic protein (VPGXG)n (X = V and K, n = 195), the observed conformational distribution around Pro and Gly sheds light on the molecular mechanism of elastin elasticity.
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Biomacromolecules. 2011 May 9;12(5):1546-55
Authors: Sharpe S, Simonetti K, Yau J, Walsh P
Abstract
The characterization of the molecular structure and physical properties of self-assembling peptides is an...
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09-10-2011 06:51 PM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Chem Commun (Camb). 2010 Sep 28;46(36):6714-6
Authors: Jenkins JE, Creager MS, Butler EB, Lewis RV, Yarger JL, Holland GP
Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major...
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12-28-2010 03:31 PM
[NMR paper] Conformational analysis by NMR and distance geometry techniques of a peptide mimetic
Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
Related Articles Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
J Pept Res. 2005 Feb;65(2):200-8
Authors: Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
The Antennapedia homeodomain structure consists of four helices. The helices II and III are connected by a tripeptide that...
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11-24-2010 11:14 PM
[NMR paper] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Magn Reson Chem. 2004 Feb;42(2):267-75
Authors: Yao XL, Conticello VP, Hong M
Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...
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11-24-2010 09:25 PM
[NMR paper] Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysi
Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Related Articles Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Biopolymers. 2003 Oct;70(2):158-68
Authors: Hong M, Isailovic D, McMillan RA, Conticello VP
The conformation of an elastin-mimetic recombinant protein, 39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and...
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11-24-2010 09:16 PM
[NMR paper] Measurement of conformational constraints in an elastin-mimetic protein by residue-pa
Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR.
Related Articles Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR.
J Biomol NMR. 2002 Feb;22(2):175-9
Authors: Hong M, McMillan RA, Conticello VP
We introduce a solid-state NMR technique for selective detection of a residue pair in multiply labeled proteins to obtain site-specific structural constraints. The method exploits the frequency-offset dependence of cross...
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11-24-2010 08:49 PM
[NMR paper] NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Related Articles NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Biochemistry. 2002 Feb 19;41(7):2149-57
Authors: Johnson MA, Rotondo A, Pinto BM
Transferred nuclear Overhauser enhancement (TRNOE) experiments have been performed at 800 MHz to investigate the bound conformation of the hexapeptide DRPVPY, a functional molecular mimic of the group A Streptococcus cell-wall polysaccharide. The hexapeptide binds to the monoclonal...
Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-s
Linear Mode
