Magnetic resonance access to transiently formed protein complexes.

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Network representation of protein interactions-Experimental results.Quarterly intrinsic disorder digest (April-May-June, 2014).

P2860

Q39703271-DCF17EAE-AC21-4683-88A5-C37D5C0F34DD Q50787059-D4A4CFA3-1E70-4C6F-A07C-6DD4B87AC796

P2860

Magnetic resonance access to transiently formed protein complexes.

Item

http://www.wikidata.org/entity/Q41965999

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2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Magnetic resonance access to transiently formed protein complexes.

@en

type

Item

label

Magnetic resonance access to transiently formed protein complexes.

@en

prefLabel

Magnetic resonance access to transiently formed protein complexes.

@en

P1476

Magnetic resonance access to transiently formed protein complexes

@en

P2093

Christoph H Wunderlich

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

Christoph Kreutz

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

Dennis Kurzbach

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

Robert Konrat

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

Tomáš Sára

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

P2860

Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

Fully automated high-quality NMR structure determination of small 2H-enriched proteins

CD44: from adhesion molecules to signalling regulators

The role of dynamic conformational ensembles in biomolecular recognition

Slow dynamics in folded and unfolded states of an SH3 domain.

Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.

Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings.

Direct conversion of EPR dipolar time evolution data to distance distributions.

Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.

P304

115-123

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

P31

scholarly article

P356

10.1002/OPEN.201402008

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

P433

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

P478

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

P50

Thomas C Schwarz

P577

2014-06-18T00:00:00Z

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

P5875

264087614

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P698

25050230

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

P932

4101727

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

Magnetic resonance access to transiently formed protein complexes.

about

P2860

P2860

Magnetic resonance access to transiently formed protein complexes.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932