Intermediates in the folding of the membrane protein bacteriorhodopsin

P J Booth; S L Flitsch; L J Stern; D A Greenhalgh; P S Kim; H G Khorana

Intermediates in the folding of the membrane protein bacteriorhodopsin

P J Booth, S L Flitsch, L J Stern, D A Greenhalgh, P S Kim, H G Khorana

Chemistry

Research output: Contribution to journal › Article › peer-review

110 Citations (Scopus)

Abstract

Assembly of proteins within lipid bilayers is essential for the biogenesis and function of biological membranes. Little is known, however, about the underlying mechanism of assembly, and it is not clear whether it is possible to observe individual folding steps for integral membrane proteins either in vivo or in vitro. Fluorescence spectroscopy is used here to follow the time course of folding events for bacteriorhodopsin in mixed detergent/lipid micelles. Transient folding-intermediates are detected and binding of the retinal chromophore occurs at a late stage, when it binds to an apoprotein intermediate.

Original language	English
Pages (from-to)	139-43
Number of pages	5
Journal	Nature Structural Biology
Volume	2
Issue number	2
Publication status	Published - Feb 1995

Keywords

Apoproteins
Bacteriorhodopsins
Cholic Acids
Detergents
Dimyristoylphosphatidylcholine
Membrane Proteins
Micelles
Models, Molecular
Protein Binding
Protein Folding
Retinaldehyde
Schiff Bases
Sodium Dodecyl Sulfate
Spectrometry, Fluorescence

Cite this

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title = "Intermediates in the folding of the membrane protein bacteriorhodopsin",

abstract = "Assembly of proteins within lipid bilayers is essential for the biogenesis and function of biological membranes. Little is known, however, about the underlying mechanism of assembly, and it is not clear whether it is possible to observe individual folding steps for integral membrane proteins either in vivo or in vitro. Fluorescence spectroscopy is used here to follow the time course of folding events for bacteriorhodopsin in mixed detergent/lipid micelles. Transient folding-intermediates are detected and binding of the retinal chromophore occurs at a late stage, when it binds to an apoprotein intermediate.",

keywords = "Apoproteins, Bacteriorhodopsins, Cholic Acids, Detergents, Dimyristoylphosphatidylcholine, Membrane Proteins, Micelles, Models, Molecular, Protein Binding, Protein Folding, Retinaldehyde, Schiff Bases, Sodium Dodecyl Sulfate, Spectrometry, Fluorescence",

author = "Booth, {P J} and Flitsch, {S L} and Stern, {L J} and Greenhalgh, {D A} and Kim, {P S} and Khorana, {H G}",

year = "1995",

month = feb,

language = "English",

volume = "2",

pages = "139--43",

journal = "Nature Structural Biology",

issn = "1072-8368",

publisher = "Nature Publishing Group",

number = "2",

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TY - JOUR

T1 - Intermediates in the folding of the membrane protein bacteriorhodopsin

AU - Booth, P J

AU - Flitsch, S L

AU - Stern, L J

AU - Greenhalgh, D A

AU - Kim, P S

AU - Khorana, H G

PY - 1995/2

Y1 - 1995/2

N2 - Assembly of proteins within lipid bilayers is essential for the biogenesis and function of biological membranes. Little is known, however, about the underlying mechanism of assembly, and it is not clear whether it is possible to observe individual folding steps for integral membrane proteins either in vivo or in vitro. Fluorescence spectroscopy is used here to follow the time course of folding events for bacteriorhodopsin in mixed detergent/lipid micelles. Transient folding-intermediates are detected and binding of the retinal chromophore occurs at a late stage, when it binds to an apoprotein intermediate.

AB - Assembly of proteins within lipid bilayers is essential for the biogenesis and function of biological membranes. Little is known, however, about the underlying mechanism of assembly, and it is not clear whether it is possible to observe individual folding steps for integral membrane proteins either in vivo or in vitro. Fluorescence spectroscopy is used here to follow the time course of folding events for bacteriorhodopsin in mixed detergent/lipid micelles. Transient folding-intermediates are detected and binding of the retinal chromophore occurs at a late stage, when it binds to an apoprotein intermediate.

KW - Apoproteins

KW - Bacteriorhodopsins

KW - Cholic Acids

KW - Detergents

KW - Dimyristoylphosphatidylcholine

KW - Membrane Proteins

KW - Micelles

KW - Models, Molecular

KW - Protein Binding

KW - Protein Folding

KW - Retinaldehyde

KW - Schiff Bases

KW - Sodium Dodecyl Sulfate

KW - Spectrometry, Fluorescence

M3 - Article

C2 - 7749918

SN - 1072-8368

VL - 2

SP - 139

EP - 143

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 2

ER -

Intermediates in the folding of the membrane protein bacteriorhodopsin

Abstract

Keywords

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