Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β.

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Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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Conformational dynamics and al ...... Ts) studied in interleukin-1β.

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Conformational dynamics and alignment properties of loop lanthanide-binding-tags

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Conformational dynamics and al ...... Ts) studied in interleukin-1β.

@en

Conformational dynamics and alignment properties of loop lanthanide-binding-tags

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Conformational dynamics and al ...... Ts) studied in interleukin-1β.

@en

Conformational dynamics and alignment properties of loop lanthanide-binding-tags

@nl

P1476

Conformational dynamics and al ...... Ts) studied in interleukin-1β.

@en

P2093

Bianca Bodmer

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Dominic Barthelmes

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Hendrik R A Jonker

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Kai Schnorr

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Karen N Allen

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Katja Barthelmes

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P2860

Engineering encodable lanthanide-binding tags into loop regions of proteins

Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects

Double-lanthanide-binding tags for macromolecular crystallographic structure determination

A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy

Residual dipolar couplings: are multiple independent alignments always possible?

Paramagnetic tagging for protein structure and dynamics analysis.

NMR residual dipolar couplings as probes of biomolecular dynamics.

Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.

De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media.

Probing Polytopic Membrane Protein-Substrate Interactions by Luminescence Resonance Energy Transfer.

P2888

s10858-017-0118-5

P304

187-194

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P31

scholarly article

P356

10.1007/S10858-017-0118-5

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P433

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

P478

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P50

Barbara Imperiali

Harald Schwalbe

P577

2017-05-22T00:00:00Z

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P698

28534082

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