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

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Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β.

P2860

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P2860

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

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http://www.wikidata.org/entity/Q36794520

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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name

Modulating alignment of membra ...... arge of phospholipid bicelles.

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Modulating alignment of membra ...... arge of phospholipid bicelles.

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Modulating alignment of membra ...... arge of phospholipid bicelles.

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Modulating alignment of membra ...... arge of phospholipid bicelles.

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Modulating alignment of membra ...... arge of phospholipid bicelles.

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Modulating alignment of membra ...... arge of phospholipid bicelles.

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P1476

Modulating alignment of membra ...... arge of phospholipid bicelles.

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P2093

Ad Bax

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

Alexander S Maltsev

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

John M Louis

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

Justin L Lorieau

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

P2860

High-Resolution Nuclear Magnetic Resonance Spectra of Orientated Molecules

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples

The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes

NMR structures of biomolecules using field oriented media and residual dipolar couplings

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

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

P2888

s10858-013-9720-3

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369-377

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scholarly article

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10.1007/S10858-013-9720-3

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3636151

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

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P2860

P2860

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

description

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type

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P1433

P1476

P2093

P2860

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P31

P356

P433

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P5875

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P1433

P1476

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P356

P433

P478

P577

P5875

P698

P932