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Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme

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Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements : Application to methionine residues in a cavity mutant of T4 lysozyme. / Skrynnikov, N. R.; Mulder, F. A A; Hon, B. et al.

In: Journal of the American Chemical Society, Vol. 123, No. 19, 14.10.2001, p. 4556-4566.

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@article{1dca0e74fc3b4ed086728118573d6a69,
title = "Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme",
abstract = "A relaxation dispersion-based NMR experiment is presented for the measurement and quantitation of μs-ms dynamic processes at methyl side-chain positions in proteins. The experiment measures the exchange contribution to the 13C line widths of methyl groups using a constant-time CPMG scheme. The effects of cross-correlated spin relaxation between dipole-dipole and dipole-CSA interactions as well as the effects of scalar coupling responsible for mixing of magnetization modes during the course of the experiment have been investigated in detail both theoretically and through simulations. It is shown that the complex relaxation properties of the methyl spin system do not complicate extraction of accurate exchange parameters as long as care is taken to ensure that appropriate magnetization modes are interchanged in the middle of the constant-time CPMG period. An application involving the measurement of relaxation dispersion profiles of methionine residues in a Leu99Ala substitution of T4 lysozyme is presented. All of the methionine residues are sensitive to an exchange event with a rate on the order of 1200 s-1 at 20 °C that may be linked to a process in which hydrophobic ligands are able to rapidly bind to the cavity that is present in this mutant.",
author = "Skrynnikov, {N. R.} and Mulder, {F. A A} and B. Hon and Dahlquist, {F. W.} and Kay, {L. E.}",
year = "2001",
month = oct,
day = "14",
doi = "10.1021/ja004179p",
language = "English",
volume = "123",
pages = "4556--4566",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "19",

}

RIS

TY - JOUR

T1 - Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements

T2 - Application to methionine residues in a cavity mutant of T4 lysozyme

AU - Skrynnikov, N. R.

AU - Mulder, F. A A

AU - Hon, B.

AU - Dahlquist, F. W.

AU - Kay, L. E.

PY - 2001/10/14

Y1 - 2001/10/14

N2 - A relaxation dispersion-based NMR experiment is presented for the measurement and quantitation of μs-ms dynamic processes at methyl side-chain positions in proteins. The experiment measures the exchange contribution to the 13C line widths of methyl groups using a constant-time CPMG scheme. The effects of cross-correlated spin relaxation between dipole-dipole and dipole-CSA interactions as well as the effects of scalar coupling responsible for mixing of magnetization modes during the course of the experiment have been investigated in detail both theoretically and through simulations. It is shown that the complex relaxation properties of the methyl spin system do not complicate extraction of accurate exchange parameters as long as care is taken to ensure that appropriate magnetization modes are interchanged in the middle of the constant-time CPMG period. An application involving the measurement of relaxation dispersion profiles of methionine residues in a Leu99Ala substitution of T4 lysozyme is presented. All of the methionine residues are sensitive to an exchange event with a rate on the order of 1200 s-1 at 20 °C that may be linked to a process in which hydrophobic ligands are able to rapidly bind to the cavity that is present in this mutant.

AB - A relaxation dispersion-based NMR experiment is presented for the measurement and quantitation of μs-ms dynamic processes at methyl side-chain positions in proteins. The experiment measures the exchange contribution to the 13C line widths of methyl groups using a constant-time CPMG scheme. The effects of cross-correlated spin relaxation between dipole-dipole and dipole-CSA interactions as well as the effects of scalar coupling responsible for mixing of magnetization modes during the course of the experiment have been investigated in detail both theoretically and through simulations. It is shown that the complex relaxation properties of the methyl spin system do not complicate extraction of accurate exchange parameters as long as care is taken to ensure that appropriate magnetization modes are interchanged in the middle of the constant-time CPMG period. An application involving the measurement of relaxation dispersion profiles of methionine residues in a Leu99Ala substitution of T4 lysozyme is presented. All of the methionine residues are sensitive to an exchange event with a rate on the order of 1200 s-1 at 20 °C that may be linked to a process in which hydrophobic ligands are able to rapidly bind to the cavity that is present in this mutant.

U2 - 10.1021/ja004179p

DO - 10.1021/ja004179p

M3 - Journal article

C2 - 11457242

AN - SCOPUS:0034809982

VL - 123

SP - 4556

EP - 4566

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 19

ER -