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Resonance Energy Transfer
Förster resonance energy transfer
Förster resonance energy transfer
(FRET), fluorescence resonance energy transfer (FRET), resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores).[1] A donor chromophore, initially in its electronic excited state, may transfer energy to an acceptor chromophore through nonradiative dipole–dipole coupling.[2] The efficiency of this energy transfer is inversely proportional to the sixth power of t
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Jablonski Diagram
In molecular spectroscopy, a Jablonski diagram
Jablonski diagram
is a diagram that illustrates the electronic states of a molecule and the transitions between them. The states are arranged vertically by energy and grouped horizontally by spin multiplicity. Nonradiative transitions are indicated by squiggly arrows and radiative transitions by straight arrows. The vibrational ground states of each electronic state are indicated with thick lines, the higher vibrational states with thinner lines.[1] The diagram is named after the Polish physicist Aleksander Jabłoński.[2]Contents1 Transitions 2 See also 3 References 4 External linksTransitions[edit] Jablonski diagram
Jablonski diagram
including vibrational levels for absorbance, non-radiative decay, and fluorescence.Radiative transitions involve the absorption, if the transition occurs to a higher energy level, or the emission, in the reverse case, of a photon
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Yellow Fluorescent Protein
Yellow fluorescent protein
Yellow fluorescent protein
(YFP) is a genetic mutant of green fluorescent protein (GFP) originally derived from the jellyfish Aequorea victoria. Its excitation peak is 514 nm and its emission peak is 527 nm. Like the parent GFP, YFP is a useful tool in cell and molecular biology thanks to its properties useful for fluorescence microscopy. Three improved versions of YFP are Citrine, Venus, and Ypet. They have reduced chloride sensitivity, faster maturation, and increased brightness (defined as the product of the extinction coefficient and quantum yield). Typically, YFP serves as the acceptor for genetically-encoded FRET sensors of which the most likely donor FP is monomeric cyan fluorescent protein (mCFP)
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Biochemistry
Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms.[1] By controlling information flow through biochemical signaling and the flow of chemical energy through metabolism, biochemical processes give rise to the complexity of life
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Protein
Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɪnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues
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DNA
Deoxyribonucleic acid (/diːˈɒksɪˌraɪboʊnjuːˌkliːɪk, -ˌkleɪ-/ (listen);[1] DNA) is a molecule composed of two chains that coil around each other to form a double helix carrying genetic instructions for the development, functioning, growth and reproduction of all known organisms and many viruses. DNA
DNA
and ribonucleic acid (RNA) are nucleic acids; alongside proteins, lipids and complex carbohydrates (polysaccharides), nucleic acids are one of the four major types of macromolecules that are essential for all known forms of life. The two DNA
DNA
strands are also known as polynucleotides as they are composed of simpler monomeric units called nucleotides.[2][3] Each nucleotide is composed of one of four nitrogen-containing nucleobases (cytosine [C], guanine [G], adenine [A] or thymine [T]), a sugar called deoxyribose, and a phosphate group
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Intermolecular
Intermolecular forces (IMF) are the forces which mediate interaction between molecules, including forces of attraction or repulsion which act between molecules and other types of neighboring particles, e.g., atoms or ions. Intermolecular forces are weak relative to intramolecular forces – the forces which hold a molecule together. For example, the covalent bond, involving sharing electron pairs between atoms, is much stronger than the forces present between neighboring molecules. Both sets of forces are essential parts of force fields frequently used in molecular mechanics. The investigation of intermolecular forces starts from macroscopic observations which indicate the existence and action of forces at a molecular level
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Ligand
In coordination chemistry, a ligand[help 1] is an ion or molecule (functional group) that binds to a central metal atom to form a coordination complex. The bonding with the metal generally involves formal donation of one or more of the ligand's electron pairs. The nature of metal–ligand bonding can range from covalent to ionic. Furthermore, the metal–ligand bond order can range from one to three. Ligands are viewed as Lewis bases, although rare cases are known to involve Lewis acidic "ligands".[1][2] Metals and metalloids are bound to ligands in virtually all circumstances, although gaseous "naked" metal ions can be generated in high vacuum. Ligands in a complex dictate the reactivity of the central atom, including ligand substitution rates, the reactivity of the ligands themselves, and redox
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Photobleaching
In optics, photobleaching (sometimes termed fading) is the photochemical alteration of a dye or a fluorophore molecule such that it permanently is unable to fluoresce. This is caused by cleaving of covalent bonds or non-specific reactions between the fluorophore and surrounding molecules.[1] Such irreversible modifications in covalent bonds is caused by transition from a singlet state to the triplet state of the fluorophores. The number of excitation cycles vary to achieve full bleaching. In microscopy, photobleaching may complicate the observation of fluorescent molecules, since they will eventually be destroyed by the light exposure necessary to stimulate them into fluorescing. This is especially problematic in time-lapse microscopy. However, photobleaching may also be used prior to applying the (primarily antibody-linked) fluorescent molecules, in an attempt to quench autofluorescence
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Bandpass Filter
A band-pass filter (also bandpass filter, BPF) is a device that passes frequencies within a certain range and rejects (attenuates) frequencies outside that range.Contents1 Description 2 Q factor 3 Applications3.1 Loudspeaker enclosures3.1.1 Compound or band-pass3.2 Other fields4 See also 5 References 6 External linksDescription[edit] An example of an analogue electronic band-pass filter is an RLC circuit (a resistor–inductor–capacitor circuit). These filters can also be created by combining a low-pass filter with a high-pass filter.[1] Bandpass is an adjective that describes a type of filter or filtering process; it is to be distinguished from passband, which refers to the actual portion of affected spectrum
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Fluorescence-lifetime Imaging Microscopy
Fluorescence-lifetime imaging microscopy or FLIM is an imaging technique for producing an image based on the differences in the exponential decay rate of the fluorescence from a fluorescent sample. It can be used as an imaging technique in confocal microscopy, two-photon excitation microscopy, and multiphoton tomography. The lifetime of the fluorophore signal, rather than its intensity, is used to create the image in FLIM
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Cyan Fluorescent Protein
The green fluorescent protein (GFP) is a protein composed of 238 amino acid residues (26.9 kDa) that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range.[2][3] Although many other marine organisms have similar green fluorescent proteins, GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria. The GFP from A. victoria has a major excitation peak at a wavelength of 395 nm and a minor one at 475 nm. Its emission peak is at 509 nm, which is in the lower green portion of the visible spectrum. The fluorescence quantum yield (QY) of GFP is 0.79. The GFP from the sea pansy (Renilla reniformis) has a single major excitation peak at 498 nm
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Green Fluorescent Protein
The green fluorescent protein (GFP) is a protein composed of 238 amino acid residues (26.9 kDa) that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range.[2][3] Although many other marine organisms have similar green fluorescent proteins, GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria. The GFP from A. victoria has a major excitation peak at a wavelength of 395 nm and a minor one at 475 nm. Its emission peak is at 509 nm, which is in the lower green portion of the visible spectrum. The fluorescence quantum yield (QY) of GFP is 0.79. The GFP from the sea pansy (Renilla reniformis) has a single major excitation peak at 498 nm
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Molecular Biology
Molecular biology
Molecular biology
/məˈlɛkjʊlər/ is a branch of biochemistry which concerns the molecular basis of biological activity between biomolecules in the various systems of a cell, including the interactions between DNA, RNA, and proteins and their biosynthesis, as well as the regulation of these interactions.[1] Writing in Nature in 1961, William Astbury described molecular biology as:"...not so much a technique as an approach, an approach from the viewpoint of the so-called basic sciences with the leading idea of searching below the large-scale manifestations of classical biology for the corresponding molecular plan. It is concerned particularly with the forms of biological molecules and [...] is predominantly three-dimensional and structural—which does not mean, however, that it is merely a refinement of morphology
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Genetic Engineering
Genetic engineering, also called genetic modification or genetic manipulation, is the direct manipulation of an organism's genes using biotechnology. It is a set of technologies used to change the genetic makeup of cells, including the transfer of genes within and across species boundaries to produce improved or novel organisms. New DNA
DNA
is obtained by either isolating and copying the genetic material of interest using recombinant DNA
DNA
methods or by artificially synthesising the DNA. A construct is usually created and used to insert this DNA into the host organism. The first recombinant DNA
DNA
molecule was made by Paul Berg
Paul Berg
in 1972 by combining DNA
DNA
from the monkey virus SV40
SV40
with the lambda virus. As well as inserting genes, the process can be used to remove, or "knock out", genes
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Protease
A protease (also called a peptidase or proteinase) is an enzyme that performs proteolysis; protein catabolism by hydrolysis of peptide bonds. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms
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