Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.

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Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.Influence of glutamic acid residues and pH on the properties of transmembrane helices.

P2860

Q31116183-CB4451FC-E92C-439F-9E76-D1046527A326 Q51204462-008DC07C-35DC-4294-81FC-9CCD1A1CF240

P2860

Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.

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http://www.wikidata.org/entity/Q36763187

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

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2016年论文

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name

Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

@ast

Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

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type

Item

label

Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

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Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

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prefLabel

Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

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Juxta-terminal Helix Unwinding ...... mics of Transmembrane Helices.

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P1476

Juxta-terminal Helix Unwinding ...... amics of Transmembrane Helices

@en

P2093

Armin Mortazavi

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

Kelsey A Sparks

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

P2860

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain

Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution

Experimentally determined hydrophobicity scale for proteins at membrane interfaces

Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR

Comparisons of interfacial Phe, Tyr, and Trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides.

The preference of tryptophan for membrane interfaces.

Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments.

On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics

Charged or aromatic anchor residue dependence of transmembrane peptide tilt.

Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using X-ray scattering from oriented multilamellar arrays and from unilamellar vesicles.

P304

462-465

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P31

scholarly article

P356

10.1002/CBIC.201500656

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P433

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

P478

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

P50

Denise V Greathouse

Roger E Koeppe

Venkatesan Rajagopalan

P577

2016-02-10T00:00:00Z

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P698

26749271

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P921

transmembrane protein

P932

4820057

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Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.

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P2860

P2860

Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932