Folding alpha-helical membrane proteins: kinetic studies on bacteriorhodopsin. (Q41679930)

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8 November 2019

review article

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title

Folding alpha-helical membrane proteins: kinetic studies on bacteriorhodopsin (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427005%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

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1

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8 November 2019

author name string

Booth PJ

series ordinal

1

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7 October 2017

publication date

1 January 1997

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8 November 2019

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8 November 2019

volume

2

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8 November 2019

issue

6

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8 November 2019

page(s)

R85-92

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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

8 November 2019

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Intermediates in the folding of the membrane protein bacteriorhodopsin

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Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed inEscherichia coli

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Assembly of Light-Harvesting Chlorophylla/bComplexin Vitro. Time-Resolved Fluorescence Measurements†

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Molecular Architecture and Electrostatic Properties of a Bacterial Porin

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Crystal structures explain functional properties of two E. coli porins

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Kinetics of folding and membrane insertion of a beta-barrel membrane protein.

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Electron-crystallographic refinement of the structure of bacteriorhodopsin

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Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process

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Bacteriorhodopsin can be refolded from two independently stable transmembrane helixes and the complementary five-helix fragment

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Membrane protein folding and oligomerization: the two-stage model

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Slow α Helix Formation during Folding of a Membrane Protein†

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Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy

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Refolding and oriented insertion of a membrane protein into a lipid bilayer

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Refolding and proton pumping activity of a polyethylene glycol-bacteriorhodopsin water-soluble conjugate

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A poly(ethylene glycol) water-soluble conjugate of porin: refolding to the native state

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7 January 2021

Retinal Binding during Folding and Assembly of the Membrane Protein Bacteriorhodopsin†

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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Pathways of protein folding

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Kinetic role of early intermediates in protein folding

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The joys of in vitro selection: chemically dressing oligonucleotides to satiate protein targets

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Evidence That Bilayer Bending Rigidity Affects Membrane Protein Folding†

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Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles

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Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

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Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective

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Structure of the inverted hexagonal (HII) phase, and non-lamellar phase transitions of lipids

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Lateral pressure in membranes

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Measuring the elastic parameters for inverse bicontinuous cubic phases

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Lipidic cubic phases: a novel concept for the crystallization of membrane proteins

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Specificity and promiscuity in membrane helix interactions

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A transmembrane helix dimer: structure and implications

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7 January 2021

Studies on the Retinal-Protein Interaction in Bacteriorhodopsin

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7 January 2021

Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin

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Pigments induce folding of light-harvesting chlorophyll a/b-binding protein

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427005%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

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