Related ArticlesA Solid-State (17)O NMR Study of l-Tyrosine in Different Ionization States: Implications for Probing Tyrosine Side Chains in Proteins.
J Phys Chem B. 2010 Aug 16;
Authors: Zhu J, Lau JY, Wu G
We report experimental characterization of (17)O quadrupole coupling (QC) and chemical shift (CS) tensors for the phenolic oxygen in three l-tyrosine (l-Tyr) compounds: l-Tyr, l-Tyr.HCl, and Na(2)(l-Tyr). This is the first time that these fundamental (17)O NMR tensors are completely determined for phenolic oxygens in different ionization states. We find that, while the (17)O QC tensor changes very little upon phenol ionization, the (17)O CS tensor displays a remarkable sensitivity. In particular, the isotropic (17)O chemical shift increases by approximately 60 ppm upon phenol ionization, which is 6 times larger than the corresponding change in the isotropic (13)C chemical shift for the C(zeta) nucleus of the same phenol group. By examining the CS tensor orientation in the molecular frame of reference, we discover a "cross-over" effect between delta(11) and delta(22) components for both (17)O and (13)C CS tensors. We demonstrate that the knowledge of such "cross-over" effects is crucial for understanding the relationship between the observed CS tensor components and chemical bonding. Our results suggest that solid-state (17)O NMR can potentially be used to probe the ionization state of tyrosine side chains in proteins.
PMID: 20712305 [PubMed - as supplied by publisher]
Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase
Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase
Abstract We have developed NMR spectroscopic methods to investigate the tyrosines within Bacillus circulans xylanase (BcX). Four slowly exchanging buried tyrosine hydroxyl protons with chemical shifts between 7.5 and 12.5 ppm were found using a long-range 13C-HSQC experiment that exploits the 3JCH coupling between the ring 1Hη and 13Cε nuclei. The NMR signals from these protons were assigned via 13C-tyrosine selective labelling and a suite of scalar and 13C,15N-filtered/edited NOE...
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[NMR paper] 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of
15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
Related Articles 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
J Magn Reson. 2005 Apr;173(2):322-7
Authors: Chekmenev EY, Hu J, Gor'kov PL, Brey WW, Cross TA, Ruuge A, Smirnov AI
This communication reports the first...
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[NMR paper] Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR a
Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Related Articles Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Magn Reson Chem. 2004 Feb;42(2):258-66
Authors: Asakura T, Suita K, Kameda T, Afonin S, Ulrich AS
The influence of the bulky and H-bonding Tyr side-chain on its Ala- and Gly-rich environment in Bombyx mori silk fibroin was...
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11-24-2010 09:25 PM
[NMR paper] A solid-state NMR study of protein hydration and stability.
A solid-state NMR study of protein hydration and stability.
Related Articles A solid-state NMR study of protein hydration and stability.
Pharm Res. 1998 Dec;15(12):1816-21
Authors: Separovic F, Lam YH, Ke X, Chan HK
PURPOSE: The mobility of protein in powders at different hydration levels was studied in relation to aggregation and activity. METHODS: Magic angle spinning 13C, 15N, 1H, 2H, and 17O NMR techniques were used to determine changes in the mobility of surface residues in proteins as a function of hydration and related to changes in...
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[NMR paper] Dynamic structure of proteins in solid state. 1H and 13C NMR relaxation study.
Dynamic structure of proteins in solid state. 1H and 13C NMR relaxation study.
Related Articles Dynamic structure of proteins in solid state. 1H and 13C NMR relaxation study.
J Biomol Struct Dyn. 1996 Oct;14(2):211-24
Authors: Krushelnitsky AG, Fedotov VD, Spevacek J, Straka J
Temperature dependencies of 1H non-selective NMR T1 and T2 relaxation times measured at two resonance frequencies and natural abundance 13C NMR relaxation times T1 and T1r measured at room temperature have been studied in a set of dry and wet solid proteins - Bacterial...
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[NMR paper] 13C NMR determination of the tautomeric and ionization states of folate in its comple
13C NMR determination of the tautomeric and ionization states of folate in its complexes with Lactobacillus casei dihydrofolate reductase.
Related Articles 13C NMR determination of the tautomeric and ionization states of folate in its complexes with Lactobacillus casei dihydrofolate reductase.
Biochemistry. 1993 Jul 13;32(27):6846-54
Authors: Cheung HT, Birdsall B, Frenkiel TA, Chau DD, Feeney J
13C NMR studies provide a convenient way of obtaining detailed information about tautomeric and ionization states in protein-ligand complexes provided...
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[NMR paper] Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Related Articles Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Biochemistry. 1990 Jul 24;29(29):6873-83
Authors: de Groot HJ, Smith SO, Courtin J, van den Berg E, Winkel C, Lugtenburg J, Griffin RG, Herzfeld J
The visible absorption of bacteriorhodopsin (bR) is highly sensitive to pH, the maximum shifting from 568 nm (pH 7) to approximately 600 nm (pH 2) and back to 565 nm (pH 0) as the pH is decreased further with HCl. Blue membrane...
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[NMR paper] Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
Related Articles Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
Biochemistry. 1990 Jun 12;29(23):5567-74
Authors: Herzfeld J, Das Gupta SK, Farrar MR, Harbison GS, McDermott AE, Pelletier SL, Raleigh DP, Smith SO, Winkel C, Lugtenburg J
Solid-state 13C MAS NMR spectra were obtained for dark-adapted bacteriorhodopsin (bR) labeled with Tyr. Difference spectra (labeled minus natural abundance) taken at pH values between 2 and...
A Solid-State (17)O NMR Study of l-Tyrosine in Different Ionization States: Implicati
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