Subtended angleIn geometry, an angle is subtended by an arc, line segment or any other section of a curve when its two rays pass through the endpoints of that arc, line segment or curve section. Conversely, the arc, line segment or curve section confined within the rays of an angle is regarded as the corresponding subtension of that angle. It is also sometimes said that an arc is intercepted or enclosed by that angle. The precise meaning varies with context. For example, one may speak of the angle subtended by an arc of a circle when the angle's vertex is the centre of the circle.
AngleIn Euclidean geometry, an angle is the figure formed by two rays, called the sides of the angle, sharing a common endpoint, called the vertex of the angle. Angles formed by two rays are also known as plane angles as they lie in the plane that contains the rays. Angles are also formed by the intersection of two planes; these are called dihedral angles. Two intersecting curves may also define an angle, which is the angle of the rays lying tangent to the respective curves at their point of intersection.
Phase (waves)In physics and mathematics, the phase (symbol φ or φ) of a wave or other periodic function of some real variable (such as time) is an angle-like quantity representing the fraction of the cycle covered up to . It is expressed in such a scale that it varies by one full turn as the variable goes through each period (and goes through each complete cycle). It may be measured in any angular unit such as degrees or radians, thus increasing by 360° or as the variable completes a full period.
SignalIn signal processing, a signal is a function that conveys information about a phenomenon. Any quantity that can vary over space or time can be used as a signal to share messages between observers. The IEEE Transactions on Signal Processing includes audio, video, speech, , sonar, and radar as examples of signals. A signal may also be defined as observable change in a quantity over space or time (a time series), even if it does not carry information.
Ramachandran plotIn biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino acid residues in protein structure. The figure on the left illustrates the definition of the φ and ψ backbone dihedral angles (called φ and φ' by Ramachandran).
Interferometric visibilityThe interferometric visibility (also known as interference visibility and fringe visibility, or just visibility when in context) is a measure of the contrast of interference in any system subject to wave superposition. Examples include as optics, quantum mechanics, water waves, sound waves, or electrical signals. Visibility is defined as the ratio of the amplitude of the interference pattern to the sum of the powers of the individual waves. The interferometric visibility gives a practical way to measure the coherence of two waves (or one wave with itself).
InterferometryInterferometry is a technique which uses the interference of superimposed waves to extract information. Interferometry typically uses electromagnetic waves and is an important investigative technique in the fields of astronomy, fiber optics, engineering metrology, optical metrology, oceanography, seismology, spectroscopy (and its applications to chemistry), quantum mechanics, nuclear and particle physics, plasma physics, biomolecular interactions, surface profiling, microfluidics, mechanical stress/strain measurement, velocimetry, optometry, and making holograms.
PeptidePeptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides which have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others.
Non-covalent interactionIn chemistry, a non-covalent interaction differs from a covalent bond in that it does not involve the sharing of electrons, but rather involves more dispersed variations of electromagnetic interactions between molecules or within a molecule. The chemical energy released in the formation of non-covalent interactions is typically on the order of 1–5 kcal/mol (1000–5000 calories per 6.02 molecules). Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects.
Nuclear Overhauser effectThe nuclear Overhauser effect (NOE) is the transfer of nuclear spin polarization from one population of spin-active nuclei (e.g. 1H, 13C, 15N etc.) to another via cross-relaxation. A phenomenological definition of the NOE in nuclear magnetic resonance spectroscopy (NMR) is the change in the integrated intensity (positive or negative) of one NMR resonance that occurs when another is saturated by irradiation with an RF field. The change in resonance intensity of a nucleus is a consequence of the nucleus being close in space to those directly affected by the RF perturbation.
Nuclear magnetic resonance spectroscopyNuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. This spectroscopy is based on the measurement of absorption of electromagnetic radiations in the radio frequency region from roughly 4 to 900 MHz. Absorption of radio waves in the presence of magnetic field is accompanied by a special type of nuclear transition, and for this reason, such type of spectroscopy is known as Nuclear Magnetic Resonance Spectroscopy.
Peptide synthesisIn organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another. Protecting group strategies are usually necessary to prevent undesirable side reactions with the various amino acid side chains. Chemical peptide synthesis most commonly starts at the carboxyl end of the peptide (C-terminus), and proceeds toward the amino-terminus (N-terminus).
