Site-specific labeling of proteins with NMR-active unnatural amino acids (Q37577622)

21 August 2017

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title

Site-specific labeling of proteins with NMR-active unnatural amino acids (English)

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21 August 2017

7

Peter G Schultz

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21 August 2017

1

David H Jones

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21 August 2017

Bernhard H Geierstanger

9

object named as

Bernhard H Geierstanger

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21 August 2017

8

Tetsuo Uno

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21 August 2017

Susan E Cellitti

2

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21 August 2017

Xueshi Hao

3

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21 August 2017

Qiong Zhang

4

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21 August 2017

Michael Jahnz

5

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21 August 2017

Daniel Summerer

6

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21 August 2017

publication date

9 August 2009

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Journal of Biomolecular NMR

21 August 2017

published in

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21 August 2017

volume

46

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21 August 2017

issue

1

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21 August 2017

page(s)

89-100

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Protein global fold determination using site-directed spin and isotope labeling

21 August 2017

cites work

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In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR.

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Unnatural amino acid mutagenesis of green fluorescent protein

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Polychromatic selective population inversion for TROSY experiments with large proteins

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Spin label enhanced NMR screening

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The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status

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New tools provide new insights in NMR studies of protein dynamics

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The second decade--into the third millenium

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Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins

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Ligand-induced conformational heterogeneity of cytochrome P450 CYP119 identified by 2D NMR spectroscopy with the unnatural amino acid (13)C-p-methoxyphenylalanine.

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A genetically encoded photocaged tyrosine

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High-resolution multi-dimensional NMR spectroscopy of proteins in human cells.

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Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR).

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Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder.

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Spin labeling of proteins

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An expanding genetic code

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A genetically encoded fluorescent amino acid.

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Genetic incorporation of unnatural amino acids into proteins in mammalian cells

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The preparation of 19F-labeled proteins for NMR studies

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Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data

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Optimal isotope labelling for NMR protein structure determinations.

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In-cell NMR spectroscopy

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Methyl groups as probes for proteins and complexes in in-cell NMR experiments

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12 December 2020

10.1007/S10858-009-9365-4

Identifiers

DOI

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21 August 2017

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