|
Self-assembling Peptide
Self-assembling peptides are a category of peptides which undergo spontaneous assembling into ordered nanostructures. Originally described in 1993, these designer peptides have attracted interest in the field of nanotechnology for their potential for application in areas such as biomedical nanotechnology, tissue cell culturing, molecular electronics, and more. Effectively self-assembling peptides act as building blocks for a wide range of material and device applications. The essence of this technology is to replicate what nature does: to use molecular recognition processes to form ordered assemblies of building blocks that are capable of conducting biochemical activities. Background Peptides are able to perform as excellent building blocks for a wide range of materials as they can be designed to combine with a range of other building blocks such as lipids, sugars, nucleic acids, metallic nanocrystals and so on; this gives the peptides an edge over carbon nanotubes, which are ano ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Secondary Structure
Protein secondary structure is the three dimensional conformational isomerism, form of ''local segments'' of proteins. The two most common Protein structure#Secondary structure, secondary structural elements are alpha helix, alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein protein folding, folds into its three dimensional protein tertiary structure, tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the Amine, amino hydrogen and carboxyl oxygen atoms in the peptide backbone chain, backbone. Secondary structure may alternatively be defined based on the regular pattern of backbone Dihedral angle#Dihedral angles of proteins, dihedral angles in a particular region of the Ramachandran plot regardless of whether it has the correct hydrogen bonds. The concept of secondary structure was first introduced by Kaj Ulrik ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Computer
A computer is a machine that can be programmed to Execution (computing), carry out sequences of arithmetic or logical operations (computation) automatically. Modern digital electronic computers can perform generic sets of operations known as Computer program, programs. These programs enable computers to perform a wide range of tasks. A computer system is a nominally complete computer that includes the Computer hardware, hardware, operating system (main software), and peripheral equipment needed and used for full operation. This term may also refer to a group of computers that are linked and function together, such as a computer network or computer cluster. A broad range of Programmable logic controller, industrial and Consumer electronics, consumer products use computers as control systems. Simple special-purpose devices like microwave ovens and remote controls are included, as are factory devices like industrial robots and computer-aided design, as well as general-purpose devi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Microscope
An electron microscope is a microscope that uses a beam of accelerated electrons as a source of illumination. As the wavelength of an electron can be up to 100,000 times shorter than that of visible light photons, electron microscopes have a higher resolving power than light microscopes and can reveal the structure of smaller objects. A scanning transmission electron microscope has achieved better than 50 pm resolution in annular dark-field imaging mode and magnifications of up to about 10,000,000× whereas most light microscopes are limited by diffraction to about 200 nm resolution and useful magnifications below 2000×. Electron microscopes use shaped magnetic fields to form electron optical lens systems that are analogous to the glass lenses of an optical light microscope. Electron microscopes are used to investigate the ultrastructure of a wide range of biological and inorganic specimens including microorganisms, cells, large molecules, biopsy samples, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scattering
Scattering is a term used in physics to describe a wide range of physical processes where moving particles or radiation of some form, such as light or sound, are forced to deviate from a straight trajectory by localized non-uniformities (including particles and radiation) in the medium through which they pass. In conventional use, this also includes deviation of reflected radiation from the angle predicted by the law of reflection. Reflections of radiation that undergo scattering are often called ''diffuse reflections'' and unscattered reflections are called ''specular'' (mirror-like) reflections. Originally, the term was confined to light scattering (going back at least as far as Isaac Newton in the 17th century). As more "ray"-like phenomena were discovered, the idea of scattering was extended to them, so that William Herschel could refer to the scattering of "heat rays" (not then recognized as electromagnetic in nature) in 1800. John Tyndall, a pioneer in light scattering researc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Atomic Force Microscope
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 diffraction-limited system, optical diffraction limit. Overview Atomic force microscopy (AFM) is a type of scanning probe microscopy (SPM), with demonstrated resolution on the order of fractions of a nanometer, more than 1000 times better than the diffraction limited, optical diffraction limit. The information is gathered 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 The AFM has three major abilities: force measurement, topographic imaging, and manipulation. In force measurement, AFMs can be used to measure the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
β-amyloid
Amyloid beta (Aβ or Abeta) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. The peptides derive from the amyloid precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol-dependent process and substrate presentation. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers (known as "seeds") can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold. A study has suggested that APP and its amyloid potential is of ancient origins, dating as far back a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diphenylalanine
Diphenylalanine is a term that has recently been used to describe the unnatural amino acid similar to the two amino acids alanine and phenylalanine. It has been used for the synthesis of pseudopeptide analogues which are capable of inhibiting certain enzymes. Individual enantiomers of this compound can be synthesized via electrophilic amination of a chiral oxazolidinone derivative of 3,3-diphenylpropanoic acid. A historical use of the term ''diphenylalanine'' refers to the dipeptide A dipeptide is an organic compound derived from two amino acids. The constituent amino acids can be the same or different. When different, two isomers of the dipeptide are possible, depending on the sequence. Several dipeptides are physiologicall ... of phenylalanine (). References Amino acids {{amine-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide Synthesis
In 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). Protein biosynthesis (long peptides) in living organisms occurs in the opposite direction. The chemical synthesis of peptides can be carried out using classical solution-phase techniques, although these have been replaced in most research and development settings by solid-phase methods (see below). Solution-phase synthesis retains its usefulness in large-scale production of peptides for industrial purposes how ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ionic Bond
Ionic bonding is a type of chemical bonding that involves the electrostatic attraction between oppositely charged ions, or between two atoms with sharply different electronegativities, and is the primary interaction occurring in ionic compounds. It is one of the main types of bonding along with covalent bonding and metallic bonding. Ions are atoms (or groups of atoms) with an electrostatic charge. Atoms that gain electrons make negatively charged ions (called anions). Atoms that lose electrons make positively charged ions (called cations). This transfer of electrons is known as electrovalence in contrast to covalence. In the simplest case, the cation is a metal atom and the anion is a nonmetal atom, but these ions can be of a more complex nature, e.g. molecular ions like or . In simpler words, an ionic bond results from the transfer of electrons from a metal to a non-metal in order to obtain a full valence shell for both atoms. It is important to recognize that ''clean'' ionic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Van Der Waals Force
In molecular physics, the van der Waals force is a distance-dependent interaction between atoms or molecules. Unlike ionic or covalent bonds, these attractions do not result from a chemical electronic bond; they are comparatively weak and therefore more susceptible to disturbance. The van der Waals force quickly vanishes at longer distances between interacting molecules. Named after Dutch physicist Johannes Diderik van der Waals, the van der Waals force plays a fundamental role in fields as diverse as supramolecular chemistry, structural biology, polymer science, nanotechnology, surface science, and condensed matter physics. It also underlies many properties of organic compounds and molecular solids, including their solubility in polar and non-polar media. If no other force is present, the distance between atoms at which the force becomes repulsive rather than attractive as the atoms approach one another is called the van der Waals contact distance; this phenomenon resul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
