Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Abstract A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly 13C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold via a partially structured low populated intermediate that interconverts with the folded, ground state on the millisecond time-scale....
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06-20-2011 03:31 PM
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
J Biomol NMR. 2011 Jun 18;
Authors: Hansen AL, Kay LE
A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has...
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06-18-2011 01:10 PM
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Solid State Nucl Magn Reson. 2011 Mar 23;
Authors: Mao Y, Jeong M, Wang T, Ba Y
Antifreeze proteins (AFPs) provide survival mechanism for species living in subzero environments by lowering the freezing points of their...
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04-08-2011 10:00 AM
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
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01-13-2011 12:00 PM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Jan 3;
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
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01-05-2011 09:51 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
[NMR paper] What contributions to protein side-chain dynamics are probed by NMR experiments? A mo
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
Related Articles What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
J Mol Biol. 2005 May 27;349(1):185-203
Authors: Best RB, Clarke J, Karplus M
Molecular dynamics simulations of the structurally homologous proteins TNfn3 and FNfn10 have been used to investigate the contributions to side-chain dynamics measured by NMR relaxation experiments. The...
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11-24-2010 11:14 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
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