Long-lived states in an intrinsically disordered protein domain.

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Synthesis of an isotopically labeled naphthalene derivative that supports a long-lived nuclear singlet state.Long-lived coherences: improved dispersion in the frequency domain using continuous-wave and reduced-power windowed sustaining irradiation.

P2860

Q42115245-3B94A623-14F9-4E8B-AE72-CE059D376986 Q51059729-5EF744C0-F8AF-4F0A-88F1-C3BD8EE8EBD6

P2860

Long-lived states in an intrinsically disordered protein domain.

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http://www.wikidata.org/entity/Q40976588

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2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

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2013年论文

@zh-cn

name

Long-lived states in an intrinsically disordered protein domain.

@en

type

Item

label

Long-lived states in an intrinsically disordered protein domain.

@en

prefLabel

Long-lived states in an intrinsically disordered protein domain.

@en

P1476

Long-lived states in an intrinsically disordered protein domain.

@en

P2093

C Guerniou

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

F Kateb

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

L Fernandes

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

P2860

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

NMR View: A computer program for the visualization and analysis of NMR data

Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.

Spectral density function mapping using 15N relaxation data exclusively.

NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.

Characterization of intrinsically disordered prostate associated gene (PAGE5) at single residue resolution by NMR spectroscopy

Myristoylation and membrane binding regulate c-Src stability and kinase activity

Storage of nuclear magnetization as long-lived singlet order in low magnetic field

Long-lived states to monitor protein unfolding by proton NMR

P304

729-733

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P31

scholarly article

P356

10.1002/MRC.4008

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P433

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

P478

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

P50

Miquel Pons

Ildefonso Marin-Montesinos

Paul R Vasos

P577

2013-09-22T00:00:00Z

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

P698

25941036

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

Long-lived states in an intrinsically disordered protein domain.

about

P2860

P2860

Long-lived states in an intrinsically disordered protein domain.

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