Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. - Wikidata - wikimedia - TriplyDB

Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein.

Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein.

http://www.wikidata.org/entity/Q34064987

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Quantification of helix-helix binding affinities in micelles and lipid bilayers Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus Structural basis for the function and inhibition of an influenza virus proton channel Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine Binding Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Structural basis for proton conduction and inhibition by the influenza M2 protein.Coarse-grained molecular dynamics of tetrameric transmembrane peptide bundles within a lipid bilayer.Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus.Membrane assembly of simple helix homo-oligomers studied via molecular dynamics simulations.The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels.Proton transport through influenza A virus M2 protein reconstituted in vesicles.Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel.Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.First principles design of a core bioenergetic transmembrane electron-transfer protein.The interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus.Molecular dynamics simulations of homo-oligomeric bundles embedded within a lipid bilayer Membrane proteins: a new method enters the fold Structure and function of the influenza A M2 proton channel Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness.Molecular architecture with carbohydrate functionalized β-peptides adopting 314-helical conformation.Influenza A M2 protein conformation depends on choice of model membrane.Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling.The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment.Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange.Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation.Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy.Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel.A molecular dynamics study of the formation, stability, and oligomerization state of two designed coiled coils: possibilities and limitations.Determination of membrane protein molecular weight using sedimentation equilibrium analytical ultracentrifugation.Combination of Cα-H Hydrogen Bonds and van der Waals Packing Modulates the Stability of GxxxG-Mediated Dimers in Membranes.

P2860

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P2860

Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein.

http://www.wikidata.org/entity/Q34064987

description

2002 nî lūn-bûn

@nan

2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Sequence determinants of the e ...... ane four-helix-bundle protein.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Sequence determinants of the e ...... ane four-helix-bundle protein.

@en

P2093

James D Lear

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

Kathleen P Howard

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P2860

Structure of the transmembrane region of the M2 protein H+ channel

A relationship between protein stability and protein function

A transmembrane helix dimer: structure and implications

pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

Membrane protein folding and stability: physical principles

Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy

Phospholamban: protein structure, mechanism of action, and role in cardiac function.

A new data analysis method to determine binding constants of small molecules to proteins using equilibrium analytical ultracentrifugation with absorption optics.

Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly.

The preference of tryptophan for membrane interfaces.

P304

8568-8572

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scholarly article

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10.1073/PNAS.132266099

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13

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99

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P50

William DeGrado

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2002-06-01T00:00:00Z

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11290309

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12084917

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transmembrane protein

protein folding

P932

124313

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