Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study.Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase.

P2860

Q48107074-87524038-544A-46C4-9C26-862B2FD84D75 Q51699434-3C619B06-4083-4A2A-89F8-8326F12678C7

P2860

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

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name

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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Item

label

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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prefLabel

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

@en

P1476

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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P2093

Garima Jaipuria

http://www.w3.org/2001/XMLSchema#string

Hanudatta S Atreya

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Rajashekar Varma Kadumuri

http://www.w3.org/2001/XMLSchema#string

Ramakrishna Vadrevu

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P2860

Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein–protein complex structure determination

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein

MUSIC in triple-resonance experiments: amino acid type-selective (1)H-(15)N correlations

MUSIC, selective pulses, and tuned delays: amino acid type-selective (1)H-(15)N correlations, II.

MUSIC and aromatic residues: amino acid type-selective (1)H-(15)N correlations, III.

An integrated platform for automated analysis of protein NMR structures.

NMR comparison of the native energy landscapes of DLC8 dimer and monomer.

Amino acid selective unlabeling in protein NMR spectroscopy.

P304

334-340

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P31

scholarly article

P356

10.1002/CBIC.201500513

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Abhinav Dubey

P577

2015-12-10T00:00:00Z

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P698

26662553

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Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

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P2860

P2860

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698