Proteins analysed as virtual knots. - Wikidata - wikimedia - TriplyDB

Proteins analysed as virtual knots.

Proteins analysed as virtual knots.

http://www.wikidata.org/entity/Q38958193

about

Studies of global and local entanglements of individual protein chains using the concept of knotoids Topological Models for Open-Knotted Protein Chains Using the Concepts of Knotoids and Bonded Knotoids

P2860

Q41108641-D4ED38D8-622F-4BFB-AF70-65F0BE66C9E2 Q57933673-81ED7C96-6B31-4D3C-B85C-CBEA7B690863

P2860

Proteins analysed as virtual knots.

http://www.wikidata.org/entity/Q38958193

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Proteins analysed as virtual knots.

@en

type

label

Proteins analysed as virtual knots.

@en

prefLabel

Proteins analysed as virtual knots.

@en

P1433

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P2860

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Q38958193-6DA27FDD-20EF-4FCD-94DD-F37EF74231EE

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P932

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P356

P1433

Scientific Reports

P1476

Proteins analysed as virtual knots.

@en

P2093

Alexander J Taylor

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

Keith Alexander

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

Mark R Dennis

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

P2860

Intricate knots in proteins: Function and evolution

The Protein Data Bank

Knotted proteins: A tangled tale of Structural Biology

Vortex knots in tangled quantum eigenfunctions.

Discovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked Chains

Stereo- and regioselective azide/alkyne cycloadditions in carbonic anhydrase II via tethering, monitored by crystallography and mass spectrometry

Dimerization properties of the RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesis

Understanding molecular recognition of promiscuity of thermophilic methionine adenosyltransferase sMAT fromSulfolobus solfataricus

Molecular mechanism of strict substrate specificity of an extradiol dioxygenase, DesB, derived from Sphingobium sp. SYK-6

The structure of a tetrameric α-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability

P2888

P304

42300

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

P31

scholarly article

P356

10.1038/SREP42300

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

P407

P478

7

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

P577

2017-02-13T00:00:00Z

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

P6179

1083804279

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P698

28205562

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P818

1611.06185

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P932

5304221

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