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Membrane Fluidity
In biology, membrane fluidity refers to the viscosity of the lipid bilayer of a cell membrane or a synthetic lipid membrane. Lipid packing can influence the fluidity of the membrane. Viscosity of the membrane can affect the rotation and diffusion of proteins and other bio-molecules within the membrane, thereby affecting the functions of these things. Membrane fluidity is affected by fatty acids. More specifically, whether the fatty acids are saturated or unsaturated has an effect on membrane fluidity. Saturated fatty acids have no double bonds in the hydrocarbon chain, and the maximum amount of hydrogen. The absence of double bonds increases fluidity. Unsaturated fatty acids have at least one double bond, creating a "kink" in the chain. The double bond decreases fluidity. While the addition of one double bond raises the melting temperature, research conducted by Xiaoguang Yang et. al. supports that four or more double bonds has a direct correlation to membrane fluidity. Membrane f ...
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Viscosity
Viscosity is a measure of a fluid's rate-dependent drag (physics), resistance to a change in shape or to movement of its neighboring portions relative to one another. For liquids, it corresponds to the informal concept of ''thickness''; for example, syrup has a higher viscosity than water. Viscosity is defined scientifically as a force multiplied by a time divided by an area. Thus its SI units are newton-seconds per metre squared, or pascal-seconds. Viscosity quantifies the internal friction, frictional force between adjacent layers of fluid that are in relative motion. For instance, when a viscous fluid is forced through a tube, it flows more quickly near the tube's center line than near its walls. Experiments show that some stress (physics), stress (such as a pressure difference between the two ends of the tube) is needed to sustain the flow. This is because a force is required to overcome the friction between the layers of the fluid which are in relative motion. For a tube ...
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Fluorescence Microscopy
A fluorescence microscope is an optical microscope that uses fluorescence instead of, or in addition to, scattering, reflection, and attenuation or absorption, to study the properties of organic or inorganic substances. A fluorescence microscope is any microscope that uses fluorescence to generate an image, whether it is a simple setup like an epifluorescence microscope or a more complicated design such as a confocal microscope, which uses optical sectioning to get better resolution of the fluorescence image. Principle The specimen is illuminated with light of a specific wavelength (or wavelengths) which is absorbed by the fluorophores, causing them to emit light of longer wavelengths (i.e., of a different color than the absorbed light). The illumination light is separated from the much weaker emitted fluorescence through the use of a spectral emission filter. Typical components of a fluorescence microscope are a light source (xenon arc lamp or mercury-vapor lamp are com ...
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Solid-state Physics
Solid-state physics is the study of rigid matter, or solids, through methods such as solid-state chemistry, quantum mechanics, crystallography, electromagnetism, and metallurgy. It is the largest branch of condensed matter physics. Solid-state physics studies how the large-scale properties of solid materials result from their atomic-scale properties. Thus, solid-state physics forms a theoretical basis of materials science. Along with solid-state chemistry, it also has direct applications in the technology of transistors and semiconductors. Background Solid materials are formed from densely packed atoms, which interact intensely. These interactions produce the mechanical (e.g. hardness and Elasticity (physics), elasticity), Heat conduction, thermal, Electrical conduction, electrical, Magnetism, magnetic and Crystal optics, optical properties of solids. Depending on the material involved and the conditions in which it was formed, the atoms may be arranged in a regular, geometric patt ...
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Spin Label
A spin label (SL) is an organic molecule which possesses an unpaired electron, usually on a nitrogen atom, and the ability to bind to another molecule. Spin labels are normally used as tools for probing proteins or biological membrane-local dynamics using electron paramagnetic resonance spectroscopy. The site-directed spin labeling (SDSL) technique allows one to monitor a specific region within a protein. In protein structure examinations, amino acid-specific SLs can be used. The goal of spin labeling is somewhat similar to that of isotopic substitution in NMR spectroscopy. There one replaces an atom lacking a nuclear spin (and so is NMR-silent) with an isotope having a spin (and so is NMR-active). This technique is useful for tracking the chemical environment around an atom when full substitution with an NMR-active isotope is not feasible. Recently, spin-labelling has also been used to probe chemical local environment in NMR itself, in a technique known as Paramagnetic Relaxa ...
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Nuclear Magnetic Resonance Spectroscopy
Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a Spectroscopy, spectroscopic technique based on re-orientation of Atomic nucleus, atomic nuclei with non-zero nuclear spins in an external magnetic field. This re-orientation occurs with absorption of electromagnetic radiation in the radio frequency region from roughly 4 to 900 MHz, which depends on the Isotope, isotopic nature of the nucleus and increases proportionally to the strength of the external magnetic field. Notably, the resonance frequency of each NMR-active nucleus depends on its chemical environment. As a result, NMR spectra provide information about individual functional groups present in the sample, as well as about connections between nearby nuclei in the same molecule. As the NMR spectra are unique or highly characteristic to individual compounds and functional groups, NMR spectroscopy is one of the most important methods to identify ...
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Force Spectroscopy
Force spectroscopy is a set of techniques for the study of the interactions and the binding forces between individual molecules. These methods can be used to measure the mechanical properties of single polymer molecules or proteins, or individual chemical bonds. The name "force spectroscopy", although widely used in the scientific community, is somewhat misleading, because there is no true matter-radiation interaction. Techniques that can be used to perform force spectroscopy include atomic force microscopy, optical tweezers, magnetic tweezers, acoustic force spectroscopy, microneedles, and biomembranes. Force spectroscopy measures the behavior of a molecule under stretching or torsional mechanical force. In this way a great deal has been learned in recent years about the mechanochemical coupling in the enzymes responsible for muscle contraction, transport in the cell, energy generation (F1-ATPase), DNA replication and transcription (polymerases), DNA unknotting and unwinding (to ...
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Atomic Force Microscopy
Atomic force microscopy (AFM) or scanning force microscopy (SFM) is a very-high-resolution type of scanning probe microscopy (SPM), with demonstrated resolution on the order of fractions of a nanometer, more than 1000 times better than the optical diffraction limit. Overview Atomic force microscopy (AFM) gathers information by "feeling" or "touching" the surface with a mechanical probe. Piezoelectric elements that facilitate tiny but accurate and precise movements on (electronic) command enable precise scanning. Despite the name, the Atomic Force Microscope does not use the nuclear force. Abilities and spatial resolution The AFM has three major abilities: force measurement, topographic imaging, and manipulation. In force measurement, AFMs can be used to measure the forces between the probe and the sample as a function of their mutual separation. This can be applied to perform force spectroscopy, to measure the mechanical properties of the sample, such as the sample's Youn ...
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Fluorescence
Fluorescence is one of two kinds of photoluminescence, the emission of light by a substance that has absorbed light or other electromagnetic radiation. When exposed to ultraviolet radiation, many substances will glow (fluoresce) with colored visible light. The color of the light emitted depends on the chemical composition of the substance. Fluorescent materials generally cease to glow nearly immediately when the radiation source stops. This distinguishes them from the other type of light emission, phosphorescence. Phosphorescent materials continue to emit light for some time after the radiation stops. This difference in duration is a result of quantum spin effects. Fluorescence occurs when a photon from incoming radiation is absorbed by a molecule, exciting it to a higher energy level, followed by the emission of light as the molecule returns to a lower energy state. The emitted light may have a longer wavelength and, therefore, a lower photon energy than the absorbed radi ...
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Electron Spin Resonance
Electron paramagnetic resonance (EPR) or electron spin resonance (ESR) spectroscopy is a method for studying materials that have unpaired electrons. The basic concepts of EPR are analogous to those of nuclear magnetic resonance (NMR), but the spins excited are those of the electrons instead of the atomic nuclei. EPR spectroscopy is particularly useful for studying metal complexes and organic radicals. EPR was first observed in Kazan State University by Soviet physicist Yevgeny Zavoisky in 1944, and was developed independently at the same time by Brebis Bleaney at the University of Oxford. Theory Origin of an EPR signal Every electron has a magnetic moment and spin quantum number s = \tfrac , with magnetic components m_\mathrm = + \tfrac or m_\mathrm = - \tfrac . In the presence of an external magnetic field with strength B_\mathrm , the electron's magnetic moment aligns itself either antiparallel ( m_\mathrm = - \tfrac ) or parallel ( m_\mathrm = + \tfrac ) to the fie ...
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Macromolecules
A macromolecule is a "molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass." Polymers are physical examples of macromolecules. Common macromolecules are biopolymers (nucleic acids, proteins, and carbohydrates). and polyolefins (polyethylene) and polyamides (nylon). Synthetic macromolecules Many macromolecules are synthetic polymers (plastics, synthetic fibers, and synthetic rubber. Polyethylene is produced on a particularly large scale such that ethylene is the primary product in the chemical industry. Macromolecules in nature * Proteins are polymers of amino acids joined by peptide bonds. * DNA and RNA are polymers of nucleotides joined by phosphodiester bonds. These nucleotides consist of a phosphate group, a sugar (ribose in the case of RNA, deoxyribose in the case of DNA), and a nucleotide base (either adenine, guanine, ...
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Biological Membranes
A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another. Biological membranes, in the form of eukaryotic cell membranes, consist of a phospholipid bilayer with embedded, integral and peripheral proteins used in communication and transportation of chemicals and ions. The bulk of lipids in a cell membrane provides a fluid matrix for proteins to rotate and laterally diffuse for physiological functioning. Proteins are adapted to high membrane fluidity environment of the lipid bilayer with the presence of an annular lipid shell, consisting of lipid molecules bound tightly to the surface of integral membrane proteins. The cell membranes are different from the isolating tissues formed by layers of cells, such as mucous membranes, basement membranes, and serous membranes. Composi ...
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Integral Membrane Proteins
An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents. Proteins that adhere only temporarily to cellular membranes are known as peripheral membrane proteins. These proteins can either associate with integral membrane proteins, or independently insert in the lipid bilayer in several ways. Structure Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuc ...
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