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Crystallin
In anatomy, a crystallin is a water-soluble structural protein found in the lens and the cornea of the eye accounting for the transparency of the structure. It has also been identified in other places such as the heart, and in aggressive breast cancer tumors. The physical origins of eye lens transparency and its relationship to cataract are an active area of research. Since it has been shown that lens injury may promote nerve regeneration, crystallin has been an area of neural research. So far, it has been demonstrated that crystallin β b2 (crybb2) may be a neurite-promoting factor. Function The main function of crystallins at least in the lens of the eye is probably to increase the refractive index while not obstructing light. However, this is not their only function. It has become clear that crystallins may have several metabolic and regulatory functions, both within the lens and in other parts of the body. More proteins containing βγ-crystallin domains have now been char ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lens (anatomy)
The lens, or crystalline lens, is a Transparency and translucency, transparent Biconvex lens, biconvex structure in most land vertebrate eyes. Relatively long, thin fiber cells make up the majority of the lens. These cells vary in architecture and are arranged in concentric layers. New layers of cells are recruited from a thin epithelium at the front of the lens, just below the basement membrane surrounding the lens. As a result the vertebrate lens grows throughout life. The surrounding lens membrane referred to as the lens capsule also grows in a systematic way, ensuring the lens maintains an optically suitable shape in concert with the underlying fiber cells. Thousands of suspensory ligaments are embedded into the capsule at its largest diameter which suspend the lens within the eye. Most of these lens structures are derived from the epithelium of the embryo before birth. Along with the cornea, aqueous humour, aqueous, and vitreous humours, the lens Refraction, refracts light, Fo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CRYGC
Crystallin, gamma C, also known as CRYGC, is a protein which in humans is encoded by the ''CRYGC'' gene. Function Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cataract
A cataract is a cloudy area in the lens (anatomy), lens of the eye that leads to a visual impairment, decrease in vision of the eye. Cataracts often develop slowly and can affect one or both eyes. Symptoms may include faded colours, blurry or double vision, halos around light, trouble with bright lights, and Nyctalopia, difficulty seeing at night. This may result in trouble driving, reading, or recognizing faces. Poor vision caused by cataracts may also result in an increased risk of Falling (accident), falling and Depression (mood), depression. Cataracts cause 51% of all cases of blindness and 33% of visual impairment worldwide. Cataracts are most commonly due to senescence, aging but may also occur due to Trauma (medicine), trauma or radiation exposure, be congenital cataract, present from birth, or occur following eye surgery for other problems. Risk factors include diabetes mellitus, diabetes, longstanding use of corticosteroid medication, smoking tobacco, prolonged exposu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alcohol Dehydrogenase
Alcohol dehydrogenases (ADH) () are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that are otherwise toxic, and they also participate in the generation of useful aldehyde, ketone, or alcohol groups during the biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Evolution Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. Early on in evolution, an effective method for eliminating both endogenous and exogenous fo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Anatomy
Anatomy () is the branch of morphology concerned with the study of the internal structure of organisms and their parts. Anatomy is a branch of natural science that deals with the structural organization of living things. It is an old science, having its beginnings in prehistoric times. Anatomy is inherently tied to developmental biology, embryology, comparative anatomy, evolutionary biology, and phylogeny, as these are the processes by which anatomy is generated, both over immediate and long-term timescales. Anatomy and physiology, which study the structure and function of organisms and their parts respectively, make a natural pair of related disciplines, and are often studied together. Human anatomy is one of the essential basic sciences that are applied in medicine, and is often studied alongside physiology. Anatomy is a complex and dynamic field that is constantly evolving as discoveries are made. In recent years, there has been a significant increase in the use of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Superfamily
A protein superfamily is the largest grouping (clade) of proteins for which common ancestry can be inferred (see homology (biology), homology). Usually this common ancestry is inferred from structural alignment and mechanistic similarity, even if no sequence similarity is evident. Sequence homology can then be deduced even if not apparent (due to low sequence similarity). Superfamilies typically contain several protein families which show sequence similarity within each family. The term ''protein clan'' is commonly used for protease and glycosyl hydrolases superfamilies based on the MEROPS and CAZy classification systems. Identification Superfamilies of proteins are identified using a number of methods. Closely related members can be identified by different methods to those needed to group the most evolutionarily divergent members. Sequence similarity Historically, the similarity of different amino acid sequences has been the most common method of inferring Sequence homology, h ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Elution
In analytical and organic chemistry, elution is the process of extracting one material from another by washing with a solvent: washing of loaded ion-exchange resins to remove captured ions, or eluting proteins or other biopolymers from an electrophoresis or chromatography column. In a liquid chromatography experiment, for example, an analyte is generally adsorbed by ("bound to") an adsorbent in a liquid chromatography column. The adsorbent, a solid phase, called a "stationary phase", is a powder which is coated onto a solid support. Based on an adsorbent's composition, it can have varying affinities to "hold onto" other molecules—forming a thin film on the surface of its particles. Elution then is the process of removing analytes from the adsorbent by running a solvent, called an eluent, past the adsorbent–analyte complex. As the solvent molecules "elute", or travel down through the chromatography column, they can either pass by the adsorbent–analyte complex or displac ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Size-exclusion Chromatography
Size-exclusion chromatography, also known as molecular sieve chromatography, is a chromatography, chromatographic method in which molecules in Solution (chemistry), solution are separated by their Chemical structure, shape, and in some cases molecular weight, size. It is usually applied to large molecules or macromolecular complexes such as proteins and industrial polymers. Typically, when an aqueous solution is used to transport the sample through the column, the technique is known as gel filtration chromatography, versus the name gel permeation chromatography, which is used when an organic solvent is used as a mobile phase. The chromatography column is packed with fine, porous beads which are commonly composed of dextran, agarose, or polyacrylamide polymers. The pore sizes of these beads are used to estimate the dimensions of Macromolecule, macromolecules. SEC is a widely used polymer characterization method because of its ability to provide good molar mass distribution (Mw) resul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperone (protein)
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermedi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Taxon
In biology, a taxon (back-formation from ''taxonomy''; : taxa) is a group of one or more populations of an organism or organisms seen by taxonomists to form a unit. Although neither is required, a taxon is usually known by a particular name and given a particular ranking, especially if and when it is accepted or becomes established. It is very common, however, for taxonomists to remain at odds over what belongs to a taxon and the criteria used for inclusion, especially in the context of rank-based (" Linnaean") nomenclature (much less so under phylogenetic nomenclature). If a taxon is given a formal scientific name, its use is then governed by one of the nomenclature codes specifying which scientific name is correct for a particular grouping. Initial attempts at classifying and ordering organisms (plants and animals) were presumably set forth in prehistoric times by hunter-gatherers, as suggested by the fairly sophisticated folk taxonomies. Much later, Aristotle, and later st ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SHsp
The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp). Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins. These seem to act as protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine viruses ( cyanophages). Function and regulation Hsp20, like all heat shock proteins, is in abundance when cells are under stressed conditions. Hsp20 is known to be expressed in many huma ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
