CEESY: Characterizing the conformation of unobservable protein states

Hugo Van Ingen; Geerten W. Vuister; Sybren Wijmenga; Marco Tessari

doi:10.1021/ja0568749

CEESY: Characterizing the conformation of unobservable protein states

Hugo Van Ingen, Geerten W. Vuister, Sybren Wijmenga, Marco Tessari

Radboud University Nijmegen

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these "excited states" by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states. Copyright © 2006 American Chemical Society.

Original language	English
Pages (from-to)	3856-3857
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	12
DOIs	https://doi.org/10.1021/ja0568749
Publication status	Published - 29 Mar 2006
Externally published	Yes

Keywords

amide
nitrogen
protein
proton
article
chemical exchange to excited states spectroscopy
conformational transition
correlation analysis
kinetics
nitrogen nuclear magnetic resonance
protein conformation
protein folding
proton nuclear magnetic resonance
rotation
signal detection
spectroscopy
thermodynamics
validation process

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10.1021/ja0568749

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title = "CEESY: Characterizing the conformation of unobservable protein states",

abstract = "Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these {"}excited states{"} by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states. Copyright {\textcopyright} 2006 American Chemical Society.",

keywords = "amide, nitrogen, protein, proton, article, chemical exchange to excited states spectroscopy, conformational transition, correlation analysis, kinetics, nitrogen nuclear magnetic resonance, protein conformation, protein folding, proton nuclear magnetic resonance, rotation, signal detection, spectroscopy, thermodynamics, validation process",

author = "{Van Ingen}, Hugo and Vuister, {Geerten W.} and Sybren Wijmenga and Marco Tessari",

year = "2006",

month = mar,

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doi = "10.1021/ja0568749",

language = "English",

volume = "128",

pages = "3856--3857",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

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T1 - CEESY: Characterizing the conformation of unobservable protein states

AU - Van Ingen, Hugo

AU - Vuister, Geerten W.

AU - Wijmenga, Sybren

AU - Tessari, Marco

PY - 2006/3/29

Y1 - 2006/3/29

N2 - Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these "excited states" by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states. Copyright © 2006 American Chemical Society.

AB - Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these "excited states" by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states. Copyright © 2006 American Chemical Society.

KW - amide

KW - nitrogen

KW - protein

KW - proton

KW - article

KW - chemical exchange to excited states spectroscopy

KW - conformational transition

KW - correlation analysis

KW - kinetics

KW - nitrogen nuclear magnetic resonance

KW - protein conformation

KW - protein folding

KW - proton nuclear magnetic resonance

KW - rotation

KW - signal detection

KW - spectroscopy

KW - thermodynamics

KW - validation process

U2 - 10.1021/ja0568749

DO - 10.1021/ja0568749

M3 - Article

SN - 0002-7863

VL - 128

SP - 3856

EP - 3857

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 12

ER -

CEESY: Characterizing the conformation of unobservable protein states

Abstract

Keywords

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