Ab initio study of (13)C(alpha) chemical shift anisotropy tensors in peptides (Q34674364)

3 August 2017

title

Ab initio study of (13)C(alpha) chemical shift anisotropy tensors in peptides (English)

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3 August 2017

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Jeff Birn

1

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3 August 2017

Alan Poon

series ordinal

2

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3 August 2017

Y Mao

series ordinal

3

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3 August 2017

A Ramamoorthy

series ordinal

4

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3 August 2017

language of work or name

English

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publication date

1 July 2004

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Journal of the American Chemical Society

3 August 2017

published in

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3 August 2017

volume

126

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3 August 2017

issue

27

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3 August 2017

page(s)

8529-8534

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

3 August 2017

cites work

1 reference

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The way to NMR structures of proteins

7 July 2018

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Orientation of amide-nitrogen-15 chemical shift tensors in peptides: a quantum chemical study.

7 July 2018

1 reference

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Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure

7 July 2018

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The use of chemical shifts and their anisotropies in biomolecular structure determination

7 July 2018

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Probing molecular motion by NMR

7 July 2018

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NMR studies of structure and function of biological macromolecules

7 July 2018

1 reference

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Experimental and theoretical investigation of the 13C and 15N chemical shift tensors in melanostatin-exploring the chemical shift tensor as a structural probe

26 October 2018

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26 October 2018

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C(alpha) chemical shift tensors in helical peptides by dipolar-modulated chemical shift recoupling NMR.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

Glycyl C(alpha) chemical shielding in tripeptides: measurement by solid-state NMR and correlation with X-ray structure and theory

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

Carbon-13 NMR shielding in the twenty common amino acids: comparisons with experimental results in proteins

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

Determination of calpha chemical shift tensor orientation in peptides by dipolar-modulated chemical shift recoupling NMR spectroscopy

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

An experimental and theoretical investigation of the chemical shielding tensors of (13)C(alpha) of alanine, valine, and leucine residues in solid peptides and in proteins in solution

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

Solid-state (13)C NMR chemical shift anisotropy tensors of polypeptides

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1477785

Experimental aspects of multidimensional solid-state NMR correlation spectroscopy

26 October 2018

1 reference

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Two-dimensional chemical shift/heteronuclear dipolar coupling spectra obtained with polarization inversion spin exchange at the magic angle and magic-angle sample spinning (PISEMAMAS)

26 October 2018

1 reference

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New patterns of hydrogen bonded interactions between polypeptide chains. Crystal and molecular structure of glycylglycylglycine

26 October 2018

1 reference

12 December 2020

Conformation and structure of acidic dipeptides. Crystal structures of L-alanyl-L-aspartic acid and alpha-L-glutamyl-L-aspartic acid

1 reference

12 December 2020

Structure and conformation of linear peptides. III. Structure of glycyl-glycyl-L-valine

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12 December 2020

Structure and conformation of linear peptides. V. Structure of L-prolyl-glycyl-glycine

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12 December 2020

Structure and conformation of linear peptides. XII. Structure of tryptophanyl-glycyl-glycine dihydrate

1 reference

12 December 2020

Structure and conformation of linear peptides. XIII. Structure of L-phenylalanyl-glycyl-glycine

1 reference

12 December 2020

A sequence preference for nucleation of alpha-helix--crystal structure of Gly-L-Ala-L-Val and Gly-L-Ala-L-Leu: some comments on the geometry of leucine zippers

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12 December 2020

Protein dynamics from NMR

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12 December 2020

Identifiers

DOI

10.1021/JA049879Z

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3 August 2017

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3 August 2017

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