Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors (Q43938393)

28 November 2017

title

Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors (English)

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28 November 2017

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6

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28 November 2017

7

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28 November 2017

Ladislav Benda

4

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Vladimír Sklenář

8

object named as

Vladimír Sklenář

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28 November 2017

Jiří Emmer

1

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28 November 2017

Andrea Vavrinská

2

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28 November 2017

Vladimír Sychrovský

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28 November 2017

Zdeněk Kříž

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28 November 2017

Lukáš Trantírek

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28 November 2017

publication date

1 December 2012

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Journal of Biomolecular NMR

28 November 2017

published in

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28 November 2017

volume

55

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28 November 2017

issue

1

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28 November 2017

page(s)

59-70

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CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

28 November 2017

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Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events

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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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How Does an Amide-N Chemical Shift Tensor Vary in Peptides?

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Measurement of 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning

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Two-state allosteric behavior in a single-domain signaling protein

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Basis Set Convergence of Nuclear Magnetic Shielding Constants Calculated by Density Functional Methods

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12 December 2020

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Identifiers

DOI

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Dimensions Publication ID

28 November 2017

1003769737

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