Optimal isotope labelling for NMR protein structure determinations. (Q30353197)

20 June 2017

Optimal isotope labelling for NMR protein structure determinations. (English)

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protein structure determination

20 June 2017

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author name string

Masatsune Kainosho

1

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20 June 2017

Takuya Torizawa

2

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20 June 2017

Yuki Iwashita

3

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20 June 2017

Tsutomu Terauchi

4

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20 June 2017

Akira Mei Ono

5

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20 June 2017

Peter Güntert

6

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20 June 2017

language of work or name

English

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publication date

1 March 2006

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20 June 2017

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20 June 2017

440

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20 June 2017

7080

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20 June 2017

52-57

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Role for NMR in structural genomics

20 June 2017

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NMR structure determination of proteins and protein complexes larger than 20 kDa

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The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins

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New developments in isotope labeling strategies for protein solution NMR spectroscopy

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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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Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

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High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease

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Chiral beta and random fractional deuteration for the determination of protein sidechain conformation by NMR.

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Nuclear magnetic resonance study of antibodies: a multinuclear approach

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Synthesis of (13)C/D doubly labeled L-leucines: probes for conformational analysis of the leucine side-chain.

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Efficient production of isotopically labeled proteins by cell-free synthesis: a practical protocol.

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Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis.

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In vitro synthesis of protein in microbial systems

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Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins

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1H-NMR stereospecific assignments by conformational data-base searches

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins

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Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein

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Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

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Calmodulin structure refined at 1.7 A resolution

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Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules

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

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Identifiers

DOI

10.1038/NATURE04525

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Dimensions Publication ID

20 June 2017

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