NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthase (Q33355538)

26 July 2017

title

NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthase (English)

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26 July 2017

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Leonard J Mueller

1

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26 July 2017

Michael F Dunn

series ordinal

2

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26 July 2017

language of work or name

English

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publication date

28 March 2013

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Accounts of Chemical Research

26 July 2017

published in

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26 July 2017

volume

46

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26 July 2017

issue

9

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26 July 2017

page(s)

2008-2017

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Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex

26 July 2017

cites work

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Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands

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21 June 2018

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21 June 2018

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21 June 2018

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NMR crystallography of campho[2,3-c]pyrazole (Z' = 6): combining high-resolution 1H-13C solid-state MAS NMR spectroscopy and GIPAW chemical-shift calculations

21 June 2018

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Powder crystallography by combined crystal structure prediction and high-resolution 1H solid-state NMR spectroscopy

31 October 2018

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31 October 2018

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Through-Bond 13C−13C Correlation at the Natural Abundance Level: Refining Dynamic Regions in the Crystal Structure of Vitamin-D3 with Solid-State NMR

31 October 2018

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Intermediate trapping via a conformational switch in the Na(+)-activated tryptophan synthase bienzyme complex

31 October 2018

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31 October 2018

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Solid-State NMR Crystallography through Paramagnetic Restraints

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Determination of molecular symmetry in crystalline naphthalene using solid-state NMR

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12 December 2020

Coupling of Functional Hydrogen Bonds in Pyridoxal-5‘-phosphate−Enzyme Model Systems Observed by Solid-State NMR Spectroscopy

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A Solid-State NMR Method for Solution of Zeolite Crystal Structures

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Identifiers

DOI

10.1021/AR3003333

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26 July 2017

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26 July 2017

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