NDLI: Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface.

Content Provider	PubMed Central
Author	Stoeckenius, W. Szundi, I.
Abstract	We have developed a surface model of purple membrane and applied it in an analysis of the purple-to-blue color change of bacteriorhodopsin which is induced by acidification or deionization. The model is based on dissociation and double layer theory and the known membrane structure. We calculated surface pH, ion concentrations, charge density, and potential as a function of bulk pH and concentration of mono- and divalent cations. At low salt concentrations, the surface pH is significantly lower than the bulk pH and it becomes independent of bulk pH in the deionized membrane suspension. Using an experimental acid titration curve for neutral, lipid-depleted membrane, we converted surface pH into absorption values. The calculated bacteriohodopsin color changes for acidification of purple, and titrations of deionized blue membrane with cations or base agree well with experimental results. No chemical binding is required to reproduce the experimental curves. Surface charge and potential changes in acid, base and cation titrations are calculated and their relation to the color change is discussed. Consistent with structural data, 10 primary phosphate and two basic surface groups per bacteriorhodopsin are sufficient to obtain good agreement between all calculated and experimental curves. The results provide a theoretical basis for our earlier conclusion that the purple-to-blue transition must be attributed to surface phenomena and not to cation binding at specific sites in the protein.
Related Links	http://dx.doi.org/10.1016/s0006-3495(89)82683-9
Ending Page	383
Page Count	15
Starting Page	369
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	2
Volume Number	56
Language	English
Publisher Date	1989-08-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Purple-to-blue transition of bacteriorhodopsin in a neutral lipid environment.

Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin.

Chromophore of Bacteriorhodopsin is Closer to the Cytoplasmic Surface of Purple Membrane

Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin.

Light activates rotations of bacteriorhodopsin in the purple membrane.

Location of the carboxyl terminus of bacteriorhodopsin in purple membrane.

Structural Transition of Bacteriorhodopsin Is Preceded by Deprotonation of Schiff Base: Microsecond Time-Resolved X-Ray Diffraction Study of Purple Membrane

Nature of forces stabilizing the transmembrane protein bacteriorhodopsin in purple membrane

Effects of pressure and temperature on the M412 intermediate of the bacteriorhodopsin photocycle. Implications for the phase transition of the purple membrane.

Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface.

Similar Documents

Purple-to-blue transition of bacteriorhodopsin in a neutral lipid environment.

Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin.

Chromophore of Bacteriorhodopsin is Closer to the Cytoplasmic Surface of Purple Membrane

Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin.

Light activates rotations of bacteriorhodopsin in the purple membrane.

Location of the carboxyl terminus of bacteriorhodopsin in purple membrane.

Structural Transition of Bacteriorhodopsin Is Preceded by Deprotonation of Schiff Base: Microsecond Time-Resolved X-Ray Diffraction Study of Purple Membrane

Nature of forces stabilizing the transmembrane protein bacteriorhodopsin in purple membrane

Effects of pressure and temperature on the M412 intermediate of the bacteriorhodopsin photocycle. Implications for the phase transition of the purple membrane.

Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface.