Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples (Q46397547)

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scientific article published on 2 September 2008

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English	Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples	scientific article published on 2 September 2008

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scholarly article

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples (English)

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

3

object named as

Lewis E Kay

1 reference

Europe PubMed Central

21 December 2017

author name string

Patrik Lundström

1

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

D Flemming Hansen

2

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

publication date

2 September 2008

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

Journal of Biomolecular NMR

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

42

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

1

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

35-47

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

https://scigraph.springernature.com/pub.10.1007/s10858-008-9260-4

0 references

Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton

1 reference

https://api.crossref.org/works/10.1007%2FS10858-008-9260-4

21 January 2018

Protein structure determination from NMR chemical shifts

1 reference

https://pubmed.ncbi.nlm.nih.gov/18762869

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Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do?

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https://pubmed.ncbi.nlm.nih.gov/18762869

12 December 2020

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Carbon relaxation in randomly fractionally 13C-enriched proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/18762869

12 December 2020

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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https://pubmed.ncbi.nlm.nih.gov/18762869

12 December 2020

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The mechanism of rate-limiting motions in enzyme function.

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https://pubmed.ncbi.nlm.nih.gov/18762869

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Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network

1 reference

https://pubmed.ncbi.nlm.nih.gov/18762869

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Improved labeling strategy for 13C relaxation measurements of methyl groups in proteins.

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NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements

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Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I.

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Measurement of bond vector orientations in invisible excited states of proteins

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Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements

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

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Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex

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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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Quantifying two-bond 1HN-13CO and one-bond 1H(alpha)-13C(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy

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Slow dynamics in folded and unfolded states of an SH3 domain

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Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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The dynamic energy landscape of dihydrofolate reductase catalysis

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Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

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Intrinsic dynamics of an enzyme underlies catalysis

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Mechanism of coupled folding and binding of an intrinsically disordered protein

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

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An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins

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Probing structure in invisible protein states with anisotropic NMR chemical shifts

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Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments

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Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts

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Determination of protein backbone structures from residual dipolar couplings

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Weak alignment offers new NMR opportunities to study protein structure and dynamics.

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Identifiers

10.1007/S10858-008-9260-4

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/18762869

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