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Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. / Hansen, D Flemming; Neudecker, Philipp; Vallurupalli, Pramodh et al.

In: Journal of the American Chemical Society, Vol. 132, No. 1, 13.01.2010, p. 42-43.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Hansen, DF, Neudecker, P, Vallurupalli, P, Mulder, FAA & Kay, LE 2010, 'Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion', Journal of the American Chemical Society, vol. 132, no. 1, pp. 42-43. https://doi.org/10.1021/ja909294n

APA

Hansen, D. F., Neudecker, P., Vallurupalli, P., Mulder, F. A. A., & Kay, L. E. (2010). Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society, 132(1), 42-43. https://doi.org/10.1021/ja909294n

CBE

Hansen DF, Neudecker P, Vallurupalli P, Mulder FAA, Kay LE. 2010. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society. 132(1):42-43. https://doi.org/10.1021/ja909294n

MLA

Hansen, D Flemming et al. "Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion". Journal of the American Chemical Society. 2010, 132(1). 42-43. https://doi.org/10.1021/ja909294n

Vancouver

Hansen DF, Neudecker P, Vallurupalli P, Mulder FAA, Kay LE. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society. 2010 Jan 13;132(1):42-43. https://doi.org/10.1021/ja909294n

Author

Hansen, D Flemming ; Neudecker, Philipp ; Vallurupalli, Pramodh et al. / Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. In: Journal of the American Chemical Society. 2010 ; Vol. 132, No. 1. pp. 42-43.

Bibtex

@article{a4eec8ff32e2449b85ff46bba8def487,
title = "Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion",
abstract = "Fits of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion profiles allow extraction of the kinetics and thermodynamics of exchange reactions that interconvert highly populated, ground state and low populated, excited state conformers. Structural information is also available in the form of chemical shift differences between the interconverting protein states. Here we present a very simple method for extracting chi(2) rotamer distributions of Leu side chains in 'invisible' excited protein states based on measurement of their (13)C(delta1)/(13)C(delta2) chemical shifts using methyl CPMG dispersion experiments. The methodology is applied to study the protein folding reaction of the Fyn SH3 domain. A uniform chi(2) rotamer distribution is obtained for Leu residues of the unfolded state, with each Leu occupying the trans and gauche+ conformations in a 2:1 ratio. By contrast, leucines of an 'invisible' Fyn SH3 domain folding intermediate show a much more heterogeneous distribution of chi(2) rotamer populations. The experiment provides an important tool toward the quantitative characterization of both the structural and dynamics properties of states that cannot be studied by other biophysical tools.",
keywords = "Leucine, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Proto-Oncogene Proteins c-fyn, Stereoisomerism, src Homology Domains",
author = "Hansen, {D Flemming} and Philipp Neudecker and Pramodh Vallurupalli and Mulder, {Frans A A} and Kay, {Lewis E}",
year = "2010",
month = jan,
day = "13",
doi = "10.1021/ja909294n",
language = "English",
volume = "132",
pages = "42--43",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "1",

}

RIS

TY - JOUR

T1 - Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion

AU - Hansen, D Flemming

AU - Neudecker, Philipp

AU - Vallurupalli, Pramodh

AU - Mulder, Frans A A

AU - Kay, Lewis E

PY - 2010/1/13

Y1 - 2010/1/13

N2 - Fits of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion profiles allow extraction of the kinetics and thermodynamics of exchange reactions that interconvert highly populated, ground state and low populated, excited state conformers. Structural information is also available in the form of chemical shift differences between the interconverting protein states. Here we present a very simple method for extracting chi(2) rotamer distributions of Leu side chains in 'invisible' excited protein states based on measurement of their (13)C(delta1)/(13)C(delta2) chemical shifts using methyl CPMG dispersion experiments. The methodology is applied to study the protein folding reaction of the Fyn SH3 domain. A uniform chi(2) rotamer distribution is obtained for Leu residues of the unfolded state, with each Leu occupying the trans and gauche+ conformations in a 2:1 ratio. By contrast, leucines of an 'invisible' Fyn SH3 domain folding intermediate show a much more heterogeneous distribution of chi(2) rotamer populations. The experiment provides an important tool toward the quantitative characterization of both the structural and dynamics properties of states that cannot be studied by other biophysical tools.

AB - Fits of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion profiles allow extraction of the kinetics and thermodynamics of exchange reactions that interconvert highly populated, ground state and low populated, excited state conformers. Structural information is also available in the form of chemical shift differences between the interconverting protein states. Here we present a very simple method for extracting chi(2) rotamer distributions of Leu side chains in 'invisible' excited protein states based on measurement of their (13)C(delta1)/(13)C(delta2) chemical shifts using methyl CPMG dispersion experiments. The methodology is applied to study the protein folding reaction of the Fyn SH3 domain. A uniform chi(2) rotamer distribution is obtained for Leu residues of the unfolded state, with each Leu occupying the trans and gauche+ conformations in a 2:1 ratio. By contrast, leucines of an 'invisible' Fyn SH3 domain folding intermediate show a much more heterogeneous distribution of chi(2) rotamer populations. The experiment provides an important tool toward the quantitative characterization of both the structural and dynamics properties of states that cannot be studied by other biophysical tools.

KW - Leucine

KW - Magnetic Resonance Spectroscopy

KW - Models, Molecular

KW - Protein Conformation

KW - Proto-Oncogene Proteins c-fyn

KW - Stereoisomerism

KW - src Homology Domains

U2 - 10.1021/ja909294n

DO - 10.1021/ja909294n

M3 - Journal article

C2 - 20000605

VL - 132

SP - 42

EP - 43

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 1

ER -