Relaxation studies and photoacoustic spectroscopy of bacteriorhodopsin and other molecules.

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University of Salford , Salford
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Open LibraryOL19684755M

Ulrich Haupts, Jorg Tittor and Dieter Oesterhelt () Closing in on Bacteriorhodopsin: Progress in Understanding the Molecule. Annual Review of Biophysics and Biomolecular Struct pp.

Werner Kuhlbrandt () News and Views: Bacteriorhodopsin. Rohr M., Gärtner W., Braslavsky S.E. () Laser-Induced Optoacoustic Spectroscopy (LIOAS) of Bacteriorhodopsin (BR): A Mathematical Model and Temperature Studies. In: Bićanić D. (eds) Photoacoustic and Photothermal Phenomena III.

Springer Series in Optical Sciences, vol Springer, Berlin, HeidelbergAuthor: M. Rohr, W. Gärtner, S. Braslavsky.

Role of internal water molecules in Bacteriorhodopsin Article Literature Review in Biochimica et Biophysica Acta (1) September with 44 Reads How we measure 'reads'Author: Hideki Kandori.

Journals & Books; Register Sign in. Sign in RegisterCited by: It is reviewed how nonradiative relaxation processes can be studied in the K to > K temperature range by photoacoustic spectroscopy and calorimetry.

The response of Helmholtz resonant cells is shortly by: 1. Photoacoustic spectroscopy of aromatic amino acids in proteins Article (PDF Available) in European Biophysics Journal 37(2) March. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid resid 96, and Biochemis – ().

CASCited by: The combination of high-resolution atomic force microscopy imaging and single-molecule force spectroscopy allows the identification, selection, and mechanical investigation of individual proteins. In a recent paper we had used this technique to unfold and extract single bacteriorhodopsins (BRs) from Cited by: Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy If the cycle is completely decoupled from the conformational state of other bR molecules in the membrane, then it follows that the photocycle of the all-trans component of dark-adapted PMshouldbeidentical Cited by:   Monodisperse lipid nanodiscs are particularly suitable for characterizing membrane protein in near-native environment.

To study the lipid-composition dependence of photocycle kinetics of bacteriorhodopsin (bR), transient absorption spectroscopy was utilized to monitor the evolution of the photocycle intermediates of bR reconstituted in nanodiscs Cited by: Bacteriorhodopsin is an integral membrane protein usually found in two-dimensional crystalline patches known as "purple membrane", which can occupy up to nearly 50% of the surface area of the archaeal repeating element of the hexagonal lattice is composed of three identical protein chains, each rotated by degrees relative to the others.

Active transport requires the alternation of substrate uptake and release with a switch in the access of the substrate binding site to the two sides of the membrane. Both the transfer and switch aspects of the photocycle have been subjects of magnetic resonance studies in bacteriorhodopsin.

The results for ion transfer indicate that the Schiff base of the chromophore Cited by: Please use one of the following formats to cite this article in your essay, paper or report: APA. Nanosurf Inc. (, January 26). Imaging Bacteriorhodopsin Author: Nanosurf Inc.

Bacteriorhodopsin (bR), a light-driven proton pump of Halobacterium salinarum, is known to spontaneously form a 2D-crystalline array of hexagonally oriented bR trimers in the plasma membrane patch comprised of this array is referred to as purple membrane (PM) ().It is well known that proton translocation across the membrane is achieved through the Cited by: 9.

There is a relatively long history of studies in which damage to bacteriorhodopsin (BR) structure, properties, and/or function caused by treatment with detergents has been reported. In many of these studies, a regain of lost characteristics was accomplished by replenishing with either native or foreign lipids.

It is important to distin. Bacteriorhodopsin (bR), a retinal protein in the superfamily of G-protein coupled receptors, is possibly the protein best studied by crystallography, which furnished not only high resolution structures of the protein at rest, but also detailed time-resolved images of various intermediates of its light-driven proton pump cycle.

1. Background. The integral membrane protein bacteriorhodopsin pumps protons across the membrane upon light excitation. It was discovered in the s by D. Oesterhelt and W.

Description Relaxation studies and photoacoustic spectroscopy of bacteriorhodopsin and other molecules. PDF

Stoeckenius in the purple membrane of Halobacterium salinarium [].The structure and photocycle of BR were extensively studied over the last decades and it is probably one of the Cited by: 1.

Other articles where Bacteriorhodopsin is discussed: bacteria: 16S rRNA analysis: it uses a single protein, bacteriorhodopsin, in which light energy is absorbed by retinal, a form of vitamin A, to activate a proton (hydrogen ion).

Making complements: Solid‐state MAS NMR spectra of bacteriorhodopsin in its native purple membrane environment can be used to complement crystallographic studies of the protein by validating and redefining the (possibly distorted) loop ne dihedral angles were extracted from the chemical shifts and compared to the crystal structures.

We have measured resonance Raman excitation profiles for 12 vibrational modes of light‐adapted bacteriorhodopsin using 27 excitation wavelengths ranging from to nm.

The excitation profiles are quite similar and have approximately the shape and width of the absorption spectrum. Calculations using a 29‐mode harmonic sum over states with large amounts of Cited by: Overview of attention for book Table of Contents.

Altmetric Badge. Book Overview. Chapter 4 Function-related conformational changes of protein molecules revealed by Raman spectroscopy Altmetric Badge. Chapter 5 Physical studies of Cold Denaturation of Beta-lactoglobulin.

Details Relaxation studies and photoacoustic spectroscopy of bacteriorhodopsin and other molecules. FB2

Buy Folding Pathways of Photoactive Proton Pump Bacteriorhodopsin: A detailed kinetic study involving stop-flow spectroscopy to decipher the folding pathways of Bacteriorhodopsin by Farooq, Amjad (ISBN: ) from Amazon's Book Store. Everyday low prices and free delivery on eligible : Amjad Farooq.

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The chromophore fluorescence of bacteriorhodopsin (BR) has been studied by using visible lines of an argon and He-Ne laser at room temperature. This fluorescence is extremely weak and appears as an unstructured band in the - nm : Atanaska Andreeva, Villen Kolev, Tzvetana Lazarova.

Pan, Yan, "Structure and Dynamics of the Membrane Protein Bacteriorhodopsin Studied by Mass Spectrometry" (). Electronic Thesis and Dissertation Repository. This Dissertation/Thesis is brought to you for free and open access by [email protected] It has been acceptedCited by: 1.

Fourier transform infrared and Raman spectroscopy, solid-state NMR, and X-ray crystallography have contributed detailed information about the structural changes in the proton transport cycle of the light-driven pump, bacteriorhodopsin.

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The results over the past few years add up to a step-by-step description of the configurational changes of the photoisomerized retinal, how these. bacteriorhodopsin to pump protons in response to illu- mination.

Substitution of specific amino acids in proteins provides an attractive and versatile approach to their structure-function studies. Such an approach is made possible by the techniques of recombinant DNA and is being currently used in studies of a number of proteins (1).

The study of bacteriorhodopsin (BR) and the elucidation of its function as a light driven proton pump, is only one of many examples. The first aim of this paper is to examine these materials from a technical point of view and describe how advantage can be taken of these naturally optimized systems as molecular devices in various optical Author: Christoph R.

Braeuchle. FTIR difference spectroscopy can also be used to study changes in the environment of individual water molecules in rhodopsin during the different steps in the photoactivation cascade. In this work, FTIR difference spectroscopy and amino acid isotope labeling were combined for the first time to analyze structural changes of tyrosines in rhodopsin.

On the other hand, in our studies we have mostly used low-temperature Fourier-transform infrared (FTIR) spectroscopy [22,23]. Infrared frequencies cover the 4,– cm -1 region, which corresponds to the molecular vibrations of interest, so infrared spectroscopy is a particularly suitable experimental tool to study structural changes in Cited by:.

bR Mutant Simulations et al., ; Balashov et al., ) have shown these ionic groups near retinal to control the yield of the pump. Site-directed mutagenesis has also pointed to Glu as the group responsible for accepting the proton from Asp, before releasing it to the extracellular domain (Brownet al., ; Balashov et al., ; Richter et al., ).

Mutants of bR in which.Global features of the structure and dynamics of bacteriorhodopsin are investigated using molecular modelling, dynamical simulations and neutron scattering experiments.

The simulations are performed on a model system consisting of one .Chemical shifts assignment for the unfolded state of the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant in M urea The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES studied by 2D-NMR and .