Probing slow protein dynamics by adiabatic R and R NMR experiments

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr-Purcell-Meiboom-Gill) or spin-lock R . In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing between 180° pulses or by changing the effective spin-locking field strength. In this Communication, we introduce a new method to induce a dispersion of relaxation rates. Our approach relies on altering the shape of the adiabatic full passage pulse and is conceptually different from existing approaches. By changing the nature of the adiabatic radiofrequency irradiation, we are able to obtain rotating frame R and R dispersion curves that are sensitive to slow μs/ms protein dynamics (demonstrated with ubiquitin). The strengths of this method are to (a) extend the dynamic range of the relaxation dispersion analysis, (b) avoid the need for multiple magnetic field strengths to extract dynamic parameters, (c) measure accurate relaxation rates that are independent of frequency offset, and (d) reduce the stress to NMR hardware (e.g., cryoprobes).

Original languageEnglish (US)
Pages (from-to)9979-9981
Number of pages3
JournalJournal of the American Chemical Society
Volume132
Issue number29
DOIs
StatePublished - Jul 28 2010

Fingerprint

Nuclear magnetic resonance
Proteins
Experiments
Protein Folding
Magnetic Fields
Ubiquitin
Catalysis
Protein Binding
Protein folding
Irradiation
Magnetic fields
Hardware
Communication

Cite this

Probing slow protein dynamics by adiabatic R and R NMR experiments. / Mangia, Silvia; Traaseth, Nathaniel J.; Veglia, Gianluigi; Garwood, Michael; Michaeli, Shalom.

In: Journal of the American Chemical Society, Vol. 132, No. 29, 28.07.2010, p. 9979-9981.

Research output: Contribution to journalArticle

@article{993809a9fadb487a8709bc1010607a5d,
title = "Probing slow protein dynamics by adiabatic R 1ρ and R 2ρ NMR experiments",
abstract = "Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr-Purcell-Meiboom-Gill) or spin-lock R 1ρ. In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing between 180° pulses or by changing the effective spin-locking field strength. In this Communication, we introduce a new method to induce a dispersion of relaxation rates. Our approach relies on altering the shape of the adiabatic full passage pulse and is conceptually different from existing approaches. By changing the nature of the adiabatic radiofrequency irradiation, we are able to obtain rotating frame R 1ρ and R 2ρ dispersion curves that are sensitive to slow μs/ms protein dynamics (demonstrated with ubiquitin). The strengths of this method are to (a) extend the dynamic range of the relaxation dispersion analysis, (b) avoid the need for multiple magnetic field strengths to extract dynamic parameters, (c) measure accurate relaxation rates that are independent of frequency offset, and (d) reduce the stress to NMR hardware (e.g., cryoprobes).",
author = "Silvia Mangia and Traaseth, {Nathaniel J.} and Gianluigi Veglia and Michael Garwood and Shalom Michaeli",
year = "2010",
month = "7",
day = "28",
doi = "10.1021/ja1038787",
language = "English (US)",
volume = "132",
pages = "9979--9981",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "29",

}

TY - JOUR

T1 - Probing slow protein dynamics by adiabatic R 1ρ and R 2ρ NMR experiments

AU - Mangia, Silvia

AU - Traaseth, Nathaniel J.

AU - Veglia, Gianluigi

AU - Garwood, Michael

AU - Michaeli, Shalom

PY - 2010/7/28

Y1 - 2010/7/28

N2 - Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr-Purcell-Meiboom-Gill) or spin-lock R 1ρ. In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing between 180° pulses or by changing the effective spin-locking field strength. In this Communication, we introduce a new method to induce a dispersion of relaxation rates. Our approach relies on altering the shape of the adiabatic full passage pulse and is conceptually different from existing approaches. By changing the nature of the adiabatic radiofrequency irradiation, we are able to obtain rotating frame R 1ρ and R 2ρ dispersion curves that are sensitive to slow μs/ms protein dynamics (demonstrated with ubiquitin). The strengths of this method are to (a) extend the dynamic range of the relaxation dispersion analysis, (b) avoid the need for multiple magnetic field strengths to extract dynamic parameters, (c) measure accurate relaxation rates that are independent of frequency offset, and (d) reduce the stress to NMR hardware (e.g., cryoprobes).

AB - Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr-Purcell-Meiboom-Gill) or spin-lock R 1ρ. In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing between 180° pulses or by changing the effective spin-locking field strength. In this Communication, we introduce a new method to induce a dispersion of relaxation rates. Our approach relies on altering the shape of the adiabatic full passage pulse and is conceptually different from existing approaches. By changing the nature of the adiabatic radiofrequency irradiation, we are able to obtain rotating frame R 1ρ and R 2ρ dispersion curves that are sensitive to slow μs/ms protein dynamics (demonstrated with ubiquitin). The strengths of this method are to (a) extend the dynamic range of the relaxation dispersion analysis, (b) avoid the need for multiple magnetic field strengths to extract dynamic parameters, (c) measure accurate relaxation rates that are independent of frequency offset, and (d) reduce the stress to NMR hardware (e.g., cryoprobes).

UR - http://www.scopus.com/inward/record.url?scp=77955785905&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77955785905&partnerID=8YFLogxK

U2 - 10.1021/ja1038787

DO - 10.1021/ja1038787

M3 - Article

C2 - 20590094

AN - SCOPUS:77955785905

VL - 132

SP - 9979

EP - 9981

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 29

ER -