Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Phys Chem Chem Phys. 2015 Jan 8;
Authors: Makwana KM, Mahalakshmi R
Abstract
The specific contribution of the acidic-aromatic ?-sheet favouring amino acid tyrosine to the stability of short octapeptide ?-hairpin structures is presented here. Solution NMR analysis in near-apolar environments suggests the energetically favourable mode of interaction to be T-shaped face-to-edge (FtE) and that a Trp-Tyr interacting pair is the most stabilizing. Alternate aryl geometries also exist in solution, which readily equilibrate between a preferred ?? conformation to an aromatic-amide conformation, without any change in the backbone structure. While the phenolic ring is readily accommodated at the "edge" of FtE aryl interactions, it exhibits an overall lowered contribution to scaffold stability in the "face" orientation. Such differential tyrosine interactions are key to its dual nature in proteins.
PMID: 25569770 [PubMed - as supplied by publisher]
[NMR paper] Solid-state NMR evidence for ?-hairpin structure within MAX8 designer peptide nanofibers.
Solid-state NMR evidence for ?-hairpin structure within MAX8 designer peptide nanofibers.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Solid-state NMR evidence for ?-hairpin structure within MAX8 designer peptide nanofibers.
Biophys J. 2013 Jul 2;105(1):222-30
Authors: Leonard SR, Cormier AR, Pang X, Zimmerman MI, Zhou HX, Paravastu AK
Abstract
MAX8, a designer peptide known to undergo self-assembly following changes in temperature, pH, and ionic...
nmrlearner
Journal club
0
01-30-2014 05:38 PM
[NMR paper] NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR 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...
nmrlearner
Journal club
0
06-13-2013 06:14 PM
[NMR paper] NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
Related Articles NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
J Am Chem Soc. 2005 Sep 14;127(36):12620-6
Authors: Torizawa T, Ono AM, Terauchi T, Kainosho M
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/15N-labeled...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
Related Articles The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
J Inorg Biochem. 2004 May;98(5):814-23
Authors: Berners-Price SJ, Bertini I, Gray HB, Spyroulias GA, Turano P
NMR spectroscopy was used to study the effect of guanidinium chloride on the unfolding of horse heart and yeast iso-1 cytochrome c under mild alkaline conditions. The structural changes on the horse heart protein were detected through NOESY (Nuclear Overhauser Effect...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and T
Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Related Articles Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Biochemistry. 1998 Dec 8;37(49):17318-30
Authors: Padmanabhan S, Jiménez MA, Laurents DV, Rico M
Interactions between side chains spaced (i,i + 3) and (i,i + 4) may explain the context dependence of helix propensities observed...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Structure and stability of monomeric lambda repressor: NMR evidence for two-state fol
Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Related Articles Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Biochemistry. 1995 Mar 28;34(12):3884-92
Authors: Huang GS, Oas TG
The absence of equilibrium intermediates in protein folding reactions (i.e., two-state folding) simplifies thermodynamic and kinetic analyses but is difficult to prove rigorously. We demonstrate a sensitive method for detecting partially folded species based on using proton chemical...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] 19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP recept
19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP receptor protein from E. coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP receptor protein from E. coli.
FEBS Lett. 1991 May 20;283(1):127-30
Authors: Hinds MG, King RW, Feeney J
The 19F NMR spectra of 3-fluorotyrosine containing c-AMP receptor protein (CRP) from E. coli have been recorded in the presence of...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] Nature of lysozyme-water interactions by proton NMR.
Nature of lysozyme-water interactions by proton NMR.
Related Articles Nature of lysozyme-water interactions by proton NMR.
Biochem Cell Biol. 1991 May-Jun;69(5-6):341-5
Authors: Prosser S, Peemoeller H
Proton spin-lattice relaxation measurements were performed in 10 mM lysozyme solution as a function of temperature and degree of substitution of solvent H2O with D2O. The results show that in the temperature range from 274 to 323 K, the intermolecular lysozyme proton water proton coupling contributes appreciably to the observed water proton...
Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Linear Mode
