Application of Single Molecule FRET Photon-correlation Spectroscopy to Studying DNA-Protein Interactions

2005 ◽  
Author(s):  
Samantha Fore ◽  
Thomas Huser ◽  
Rod Balhorn ◽  
Monique Cosman ◽  
Yin Yeh
Keyword(s):  
Single Molecule ◽  
Protein Interactions ◽  
Photon Correlation Spectroscopy ◽  
Correlation Spectroscopy ◽  
Photon Correlation ◽  
Single Molecule Fret ◽  
Dna Protein Interactions

scholarly journals From Femtoseconds to Hours–Measuring Dynamics over 18 Orders of Magnitude with Coherent X-rays

2021 ◽  
Vol 11 (13) ◽  
pp. 6179
Author(s):  
Felix Lehmkühler ◽  
Wojciech Roseker ◽  
Gerhard Grübel
Keyword(s):  
Time Scales ◽  
Free Electron Laser ◽  
Photon Correlation Spectroscopy ◽  
Signal To Noise Ratio ◽  
Coherent Scattering ◽  
Correlation Spectroscopy ◽  
X Rays ◽  
Photon Correlation ◽  
X Ray ◽  
Scattering Technique

X-ray photon correlation spectroscopy (XPCS) enables the study of sample dynamics between micrometer and atomic length scales. As a coherent scattering technique, it benefits from the increased brilliance of the next-generation synchrotron radiation and Free-Electron Laser (FEL) sources. In this article, we will introduce the XPCS concepts and review the latest developments of XPCS with special attention on the extension of accessible time scales to sub-μs and the application of XPCS at FELs. Furthermore, we will discuss future opportunities of XPCS and the related technique X-ray speckle visibility spectroscopy (XSVS) at new X-ray sources. Due to its particular signal-to-noise ratio, the time scales accessible by XPCS scale with the square of the coherent flux, allowing to dramatically extend its applications. This will soon enable studies over more than 18 orders of magnitude in time by XPCS and XSVS.

scholarly journals Grain Growth and Coarsening Dynamics in a Compositionally Asymmetric Block Copolymer Revealed by X-ray Photon Correlation Spectroscopy

2020 ◽  
Vol 53 (19) ◽  
pp. 8233-8243
Author(s):  
Ronald M. Lewis ◽  
Grayson L. Jackson ◽  
Michael J. Maher ◽  
Kyungtae Kim ◽  
Suresh Narayanan ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Grain Growth ◽  
Photon Correlation Spectroscopy ◽  
Correlation Spectroscopy ◽  
Photon Correlation ◽  
X Ray ◽  
Coarsening Dynamics

scholarly journals Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane

Life ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 15
Author(s):  
Radek Kaňa ◽  
Gábor Steinbach ◽  
Roman Sobotka ◽  
György Vámosi ◽  
Josef Komenda
Keyword(s):  
Membrane Proteins ◽  
Single Molecule ◽  
Protein Interactions ◽  
Thylakoid Membrane ◽  
Protein Complexes ◽  
Correlation Spectroscopy ◽  
Membrane Microdomains ◽  
Fast Diffusion ◽  
Light Harvesting Complexes ◽  
Term Survival

Biological membranes were originally described as a fluid mosaic with uniform distribution of proteins and lipids. Later, heterogeneous membrane areas were found in many membrane systems including cyanobacterial thylakoids. In fact, cyanobacterial pigment–protein complexes (photosystems, phycobilisomes) form a heterogeneous mosaic of thylakoid membrane microdomains (MDs) restricting protein mobility. The trafficking of membrane proteins is one of the key factors for long-term survival under stress conditions, for instance during exposure to photoinhibitory light conditions. However, the mobility of unbound ‘free’ proteins in thylakoid membrane is poorly characterized. In this work, we assessed the maximal diffusional ability of a small, unbound thylakoid membrane protein by semi-single molecule FCS (fluorescence correlation spectroscopy) method in the cyanobacterium Synechocystis sp. PCC6803. We utilized a GFP-tagged variant of the cytochrome b6f subunit PetC1 (PetC1-GFP), which was not assembled in the b6f complex due to the presence of the tag. Subsequent FCS measurements have identified a very fast diffusion of the PetC1-GFP protein in the thylakoid membrane (D = 0.14 − 2.95 µm2s−1). This means that the mobility of PetC1-GFP was comparable with that of free lipids and was 50–500 times higher in comparison to the mobility of proteins (e.g., IsiA, LHCII—light-harvesting complexes of PSII) naturally associated with larger thylakoid membrane complexes like photosystems. Our results thus demonstrate the ability of free thylakoid-membrane proteins to move very fast, revealing the crucial role of protein–protein interactions in the mobility restrictions for large thylakoid protein complexes.

scholarly journals Atomic Migration Studies with X-Ray Photon Correlation Spectroscopy

2014 ◽  
Vol 2 ◽  
pp. 73-94 ◽  
Author(s):  
Markus Stana ◽  
Manuel Ross ◽  
Bogdan Sepiol
Keyword(s):  
Low Temperatures ◽  
Short Range ◽  
Short Range Order ◽  
Photon Correlation Spectroscopy ◽  
Condensed Matter ◽  
Correlation Spectroscopy ◽  
Atomic Scale ◽  
Photon Correlation ◽  
X Ray ◽  
Amorphous Systems

The new technique of atomic-scale X-ray Photon Correlation Spectroscopy (aXPCS) makesuse of a coherent X-ray beam to study the dynamics of various processes in condensed matter systems.Particularly atomistic migration mechanisms are still far from being understood in most of intermetallicalloys and in amorphous systems. Special emphasis must be given to the opportunity to measureatomistic diffusion at relatively low temperatures where such measurements were far out of reach withpreviously established methods. The importance of short-range order is demonstrated on the basis ofMonte Carlo simulations.

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