(Q40576245)

21 September 2017

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title

Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins (English)

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21 September 2017

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21 September 2017

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21 September 2017

Case DA

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21 September 2017

language of work or name

English

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publication date

1 January 1994

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21 September 2017

published in

Methods in Enzymology

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21 September 2017

volume

239

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21 September 2017

page(s)

392-416

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Protein structure determination in solution by nuclear magnetic resonance spectroscopy

21 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Defining solution conformations of small linear peptides

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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7 January 2021

Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Rabbit metallothionein-2

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7 January 2021

Measurement of15N-13C J couplings in staphylococcal nuclease

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7 January 2021

Determination of heteronuclear long-range couplings to heteronuclei in natural abundance by two- and three-dimensional NMR spectroscopy

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7 January 2021

Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C

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7 January 2021

A general approach for determining scalar coupling constants in polypeptides and proteins

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7 January 2021

New nuclear magnetic resonance experiment for measurements of the vicinal coupling constants 3JHN.alpha. in proteins

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7 January 2021

Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling cons

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7 January 2021

Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy.

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7 January 2021

Determination of the phi angle in a peptide backbone by NMR spectroscopy with a combination of homonuclear and heteronuclear coupling constants.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Determining stereo-specific 1H nuclear magnetic resonance assignments from distance geometry calculations

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7 January 2021

Stereospecific assignment of leucine methyl groups with carbon-13 in natural abundance or with random 13C labeling

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7 January 2021

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

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7 January 2021

Analysis of .vphi. and .chi.1 torsion angles for hen lysozyme in solution from proton NMR spin-spin coupling constants

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7 January 2021

Accurate measurements of coupling constants from two-dimensional nuclear magnetic resonance spectra of proteins and determination of phi-angles.

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7 January 2021

Positive theta-angles in proteins by nuclear magnetic resonance spectroscopy

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7 January 2021

Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.

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7 January 2021

High-resolution solution structure of reduced French bean plastocyanin and comparison with the crystal structure of poplar plastocyanin

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7 January 2021

Structure refinement using time-averaged J-coupling constant restraints.

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7 January 2021

1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1 beta

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Quantum mechanical calculations of NMR chemical shifts in nucleic acids

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

A relational database for sequence-specific protein NMR data

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

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

1 reference

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7 January 2021

Secondary-structure dependent chemical shifts in proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sites

1 reference

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7 January 2021

Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary c

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

15N NMR assignments and chemical shift analysis of uniformly labeled15N calbindin D9kin the apo, (Cd2+)1and (Ca2+)2states

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Relationship between1H and13C NMR chemical shifts and the secondary and tertiary structure of a zinc finger peptide

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Periodic properties of proton conformational shifts in isolated protein helices. An experimental study

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

NMR chemical shifts: a tool to characterize distortions of peptide and protein helices

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shifts

1 reference

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7 January 2021

Assignment of the side-chain proton and carbon-13 resonances of interleukin-1.beta. using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Hydrogen bonding monitored by deuterium isotope effects on carbonyl 13C chemical shift in BPTI: intra-residue hydrogen bonds in antiparallel β-sheet

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

A method for the calculation of protein alpha-CH chemical shifts.

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7 January 2021

Theoretical variation of the H alpha chemical shift in acetyl-glycyl-N-methylamide and oligoglycines with molecular conformation and environment

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Empirical Comparisons of Models for Chemical-Shift Calculation in Proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Molecular Zeeman effect in formamide and the -proton chemical shift in poly(L-alanine).

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Analysis of proton chemical shifts in regular secondary structure of proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Electrostatic interactions in macromolecules: theory and applications

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https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Electrostatic Energy and Macromolecular Function

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

NMR evidence for multiple conformations in a highly helical model peptide.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2894%2939015-0

7 January 2021

10.1016/S0076-6879(94)39015-0

Identifiers

DOI

1 reference

21 September 2017

1 reference