(Q46611295)

23 December 2017

title

Off-resonance rotating-frame amide proton spin relaxation experiments measuring microsecond chemical exchange in proteins (English)

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23 December 2017

author name string

Patrik Lundström

series ordinal

1

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23 December 2017

Mikael Akke

series ordinal

2

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23 December 2017

publication date

1 June 2005

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23 December 2017

Journal of Biomolecular NMR

published in

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23 December 2017

volume

32

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23 December 2017

page(s)

163-173

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23 December 2017

issue

2

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23 December 2017

https://scigraph.springernature.com/pub.10.1007/s10858-005-5027-3

exact match

0 references

cites work

Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods.

1 reference

Crossref

https://api.crossref.org/works/10.1007%2FS10858-005-5027-3

NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis

21 January 2018

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Solution structure of calcium-free calmodulin

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Measurement of 1H T1 rho in a uniformly 15N-labeled protein in solution with heteronuclear two-dimensional spectroscopy

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12 December 2020

Structural dynamics in the C-terminal domain of calmodulin at low calcium levels

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Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor: Multisite Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Quantitative analysis of conformational exchange contributions to 1H-15N multiple-quantum relaxation using field-dependent measurements. Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant

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CPMG sequences with enhanced sensitivity to chemical exchange

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Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.

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12 December 2020

NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state.

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Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.

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Calcium-induced structural changes and domain autonomy in calmodulin

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Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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12 December 2020

Correlation between 15N NMR chemical shifts in proteins and secondary structure.

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Molecular and structural basis of target recognition by calmodulin.

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Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

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Off-resonance TROSY (R1 rho - R1) for quantitation of fast exchange processes in large proteins

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CBFbeta allosterically regulates the Runx1 Runt domain via a dynamic conformational equilibrium

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Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

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NMR characterization of the dynamics of biomacromolecules

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Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules

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Calmodulin structure refined at 1.7 A resolution

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Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations

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An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates

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12 December 2020

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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Use of chemical shifts in macromolecular structure determination

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Minimizing the effects of radio-frequency heating in multidimensional NMR experiments

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Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain

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12 December 2020

An Off-resonance Rotating Frame Relaxation Experiment for the Investigation of Macromolecular Dynamics Using Adiabatic Rotations

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12 December 2020

NMR R1 rho rotating-frame relaxation with weak radio frequency fields.

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12 December 2020

The Merck Frosst Award Lecture 1994. Calmodulin: a versatile calcium mediator protein

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Enzyme dynamics during catalysis

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12 December 2020

R1rho relaxation outside of the fast-exchange limit.

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12 December 2020

Probing multiple effects on 15N, 13C alpha, 13C beta, and 13C' chemical shifts in peptides using density functional theory

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Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains

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12 December 2020

10.1007/S10858-005-5027-3

Identifiers

DOI

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23 December 2017

PubMed ID

16034667

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23 December 2017