Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.

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Direct protein-lipid interactions shape the conformational landscape of secondary transporters CDtoolX, a downloadable software package for processing and analyses of circular dichroism spectroscopic data

P2860

Q57295402-16062CF7-E8F0-408D-B2FA-4B5F380B8E75 Q58725190-C4229947-91E3-4F2D-B762-F816D584E711

P2860

Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.

Item

http://www.wikidata.org/entity/Q50063713

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2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

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2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

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@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@en

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@nl

type

Item

label

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@en

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@nl

prefLabel

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@en

Lipid bilayer composition modu ...... ed α-helical membrane protein.

@nl

P1476

Lipid bilayer composition modu ...... ted α-helical membrane protein

@en

P2093

H E Findlay

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

M R Sanders

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

P2860

A competitive inhibitor traps LeuT in an open-to-out conformation.

Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation

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X-ray structures of LeuT in substrate-free outward-open and apo inward-open states

Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context

Structural advances for the major facilitator superfamily (MFS) transporters

Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters

Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases

Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins.

Folding and assembly of beta-barrel membrane proteins.

P304

E1799-E1808

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P31

scholarly article

P356

10.1073/PNAS.1714668115

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P407

English

P433

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

P478

115

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Paula Booth

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2018-02-05T00:00:00Z

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29432185

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P932

5828594

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Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.

about

P2860

P2860

Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932