The study of conformational states of proteins by nuclear magnetic resonance (Q39497576)

12 September 2017

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title

The study of conformational states of proteins by nuclear magnetic resonance (English)

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12 September 2017

2

Dobson CM

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12 September 2017

Campbell ID

1

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PMCID

1152695

12 September 2017

Williams RJ

series ordinal

3

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PMCID

1152695

12 September 2017

language of work or name

English

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publication date

1 October 1985

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12 September 2017

10

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inferred from page(s)

published in

Biochemical Journal

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12 September 2017

231

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12 September 2017

1

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12 September 2017

1-10

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Mechanisms of hydrogen exchange in proteins from nuclear magnetic resonance studies of individual tryptophan indole NH hydrogens in lysozyme

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Ligand-induced conformational changes in proteins

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Hydrogen exchange and structural dynamics of proteins and nucleic acids

12 September 2017

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

12 September 2017

12 December 2020

Protein conformation and proton nuclear-magnetic-resonance chemical shifts

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Identification using 1H NMR spectroscopy of slowly exchanging amide hydrogens of hen lysozyme in solution

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

A protein structure from nuclear magnetic resonance data. lac repressor headpiece

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

An NMR study of the dynamics of inhibitor‐induced conformational changes in lysozyme

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Role of proline isomerization in folding of ribonuclease A at low temperatures

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

The conformation properties of proteins in solution

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

The Application of High Resolution Nuclear Magnetic Resonance to Biological Systems

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Hydrogen exchange and the dynamic structure of proteins

12 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Nuclear magnetic resonance studies of the unfolding of pancreatic ribonuclease

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Temperature dependent molecular motion of a tyrosine residue of ferrocytochromeC

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

19F-n.m.r. studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofolate reductase. Molecular motion and coenzyme-induced conformational changes

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Quantitative Determination of Mononucleotide Conformations in Solution using Lanthanide Ion Shift and Broadening NMR Probes

15 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

On the nature of molecular conformations inferred from high-resolution NMR.

15 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Structural information from NMR secondary chemical shifts of peptide alpha C-H protons in proteins.

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes.

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Dynamics of Erabutoxin b as Studied by Nuclear Magnetic Resonance. Relaxation Studies of Methyl Proton Resonances

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1152695

Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c

21 August 2018

1 reference

12 December 2020

A structural study of the hydrophobic box region of lysozyme in solution using nuclear Overhauser effects

1 reference

12 December 2020

Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analog

1 reference

12 December 2020

Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution

1 reference

12 December 2020

Fluctuations and averaging of proton chemical shifts in the bovine pancreatic trypsin inhibitor

1 reference

12 December 2020

Proton NMR studies of denatured lysozyme

1 reference

12 December 2020

Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP complex

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ2310001

1 reference

12 September 2017

1 reference

12 September 2017

1 reference

PMCID

1152695