Thank you very much for downloading principles of fluorescence spectroscopy. As you may know, people have look hundreds times for their favorite novels like this principles of fluorescence spectroscopy, but end up in malicious downloads. Rather than reading a good book with a cup of tea in the afternoon, instead they cope with some harmful bugs inside their desktop computer. principles of fluorescence spectroscopy is available in our digital library an online access to it is set as public so you can download it instantly. Our digital library spans in multiple locations, allowing you to get the most less latency time to download any of our books like this one. Kindly say, the principles of fluorescence spectroscopy is universally compatible with any devices to read.

Principles Of Fluorescence Spectroscopy

: The unpolarized absorption and circular dichroism spectra of the fundamental vibrational transitions of the chiral molecule, 4-methyl-2-oxetanone, are calculated ab initio. Harmonic force fields are obtained using Density Functional Theory (DFT), MP2, and SCF methodologies and a 5S4P2D/3S2P (TZ2P) basis set. DFT calculations use the Local Spin Density Approximation (LSDA), BLYP, and Becke3LYP (B3LYP) density functionals. Mid-IR spectra predicted using LSDA, BLYP, and B3LYP force fields are of significantly different quality, the B3LYP force field yielding spectra in clearly superior, and overall excellent, agreement with experiment. The MP2 force field yields spectra in slightly worse agreement with experiment than the B3LYP force field. The SCF force field yields spectra in poor agreement with experiment.The basis set dependence of B3LYP force fields is also explored: the 6-31G* and TZ2P basis sets give very similar results while the 3-21G basis set yields spectra in substantially worse agreements with experiment. jg

Ab initio calculation of vibrational absorption and circular dichroism spectra using density functional force fields

Lipid Rafts: Elusive or Illusive?

Cellular plasma membranes are laterally heterogeneous, featuring a variety of distinct subcompartments that differ in their biophysical properties and composition. A large number of studies have focused on understanding the basis for this heterogeneity and its physiological relevance. The membrane raft hypothesis formalized a physicochemical principle for a subtype of such lateral membrane heterogeneity, in which the preferential associations between cholesterol and saturated lipids drive the formation of relatively packed (or ordered) membrane domains that selectively recruit certain lipids and proteins. Recent studies have yielded new insights into this mechanism and its relevance in vivo, owing primarily to the development of improved biochemical and biophysical technologies.

The mystery of membrane organization: composition, regulation and roles of lipid rafts

Endocytic recycling is coordinated with endocytic uptake to control the composition of the plasma membrane. Although much of our understanding of endocytic recycling has come from studies on the transferrin receptor, a protein internalized through clathrin-dependent endocytosis, increased interest in clathrin-independent endocytosis has led to the discovery of new endocytic recycling systems. Recent insights into the regulatory mechanisms that control endocytic recycling have focused on recycling through tubular carriers and the return to the cell surface of cargo that enters cells through clathrin-independent mechanisms. Recent work emphasizes the importance of regulated recycling in such diverse processes as cytokinesis, cell adhesion and morphogenesis, cell fusion, and learning and memory.

Pathways and mechanisms of endocytic recycling.

Niemann–Pick C1 like 1 (NPC1L1) is a sterol transporter expressed in the apical membrane of enterocytes and hepatocytes. NPC1L1 resembles the lysosomal NPC1 protein including an N-terminal domain (NTD), which binds a variety of sterols. The molecular mechanisms underlying this multiligand specificity of the NTD of NPC1L1 (NPC1L1–NTD) are not known. On the basis of the crystal structure of NPC1L1–NTD, we have investigated the structural details of protein–sterol interactions using molecular mechanics Poisson Boltzmann surface area calculations here. We found a good agreement between experimental and calculated binding affinities with similar ranking of various sterol ligands. We defined hydrogen bonding of sterol ligands via the 3′-β-hydroxy group inside the binding pose as instrumental in stabilizing the interaction. A leucine residue (LEU213) at the mouth of the binding pocket transiently opens to allow for the access of sterol into the binding pose. Our calculations also predict that NPC1L1–NTD binds po...

https://findresearcher.sdu.dk:8443/ws/files/158791405/acsomega.9b01668.pdf

Computational Modeling Explains the Multi Sterol Ligand Specificity of the N-Terminal Domain of Niemann-Pick C1-Like 1 Protein

Biophysical properties of cellular membranes critically depend on their content of cholesterol and its interaction with various other lipid species. Cholesterol-dependent friction at the nanoscale can be studied with molecular rotors, whose quantum yield depends on rotational dynamics of functional groups during their excited state lifetime. Here, we present a detailed computational analysis of a phenyl-BODIPY-linked cholesterol based molecular rotor in direct comparison with the well-known TopFluor-cholesterol. We describe a new parametrization strategy of force field parameters for the BODIPY moiety and carry out extensive molecular dynamics simulations of the probe in membranes in the absence or presence of cholesterol. Our study quantifies the extent of membrane perturbation by these probes, analyzes their tilting resistance in the bilayer and derives dynamic properties directly related to the rotor propensity. We show that phenyl-BODIPY-cholesterol bears potential as a cholesterol-dependent molecular rotor to report about microviscosity of sterol-containing model and cell membranes.

/pdf/computational-characterization-of-a-cholesterol-based-32ffjj0s27.pdf

Computational Characterization of a Cholesterol-Based Molecular Rotor in Lipid Membranes.

Direct observation of nystatin binding to the plasma membrane of living cells

The phase separation and aggregation of proteins are hallmarks of many neurodegenerative diseases. These processes can be studied in living cells using fluorescent protein constructs and quantitative live-cell imaging techniques, such as fluorescence recovery after photobleaching (FRAP) or the related fluorescence loss in photobleaching (FLIP). While the acquisition of FLIP images is straightforward on most commercial confocal microscope systems, the analysis and computational modeling of such data is challenging. Here, a novel model-free method is presented, which resolves complex spatiotemporal fluorescence-loss kinetics based on dynamic-mode decomposition (DMD) of FLIP live-cell image sequences. It is shown that the DMD of synthetic and experimental FLIP image series (DMD-FLIP) allows for the unequivocal discrimination of subcellular compartments, such as nuclei, cytoplasm, and protein condensates based on their differing transport and therefore fluorescence loss kinetics. By decomposing fluorescence-loss kinetics into distinct dynamic modes, DMD-FLIP will enable researchers to study protein dynamics at each time scale individually. Furthermore, it is shown that DMD-FLIP is very efficient in denoising confocal time series data. Thus, DMD-FLIP is an easy-to-use method for the model-free detection of barriers to protein diffusion, of phase-separated protein assemblies, and of insoluble protein aggregates. It should, therefore, find wide application in the analysis of protein transport and aggregation, in particular in relation to neurodegenerative diseases and the formation of protein condensates in living cells.

/pdf/dynamic-mode-decomposition-of-fluorescence-loss-in-3rgstlj3.pdf

Dynamic Mode Decomposition of Fluorescence Loss in Photobleaching Microscopy Data for Model-Free Analysis of Protein Transport and Aggregation in Living Cells

Daniel Wüstner

Papers

Computational Modeling Explains the Multi Sterol Ligand Specificity of the N-Terminal Domain of Niemann-Pick C1-Like 1 Protein

Computational Characterization of a Cholesterol-Based Molecular Rotor in Lipid Membranes.

Direct observation of nystatin binding to the plasma membrane of living cells

Dynamic Mode Decomposition of Fluorescence Loss in Photobleaching Microscopy Data for Model-Free Analysis of Protein Transport and Aggregation in Living Cells

Cholesterol trafficking and distribution between cellular membranes.