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Glycosidases

Secondary structure: highly patterned sub-structures alpha helix and beta sheet or of chain that assume no stable shape. Secondary structures are locally defined, meaning that there can be many different secondary motifs present in one single protein molecule.
Tertiary structure:single protein ; the spatial relationship of thecondary structural motifs to one another
Quaternary structure: the shape or structure that results from the union of more than one protein molecule, usually called subunit proteins subunits in this context, which function as part of the larger assembly or protein complex.
In addition to these evels of structure, proteins may shift between several siilar structures in performing their biological function. In the context of these functional rearrangements, these tertiary or quaternary structures are usually referred to as and transitions between them are called conformational changes.The primary structure is held together by covalent peptide bonds, which are made during the process of translation. The secondary structures are held together by hydrogen bonds. The tertiary structure is held together primarily by hydrophobic but hydrogen bonds, ionic interactions, and disulfide bonds are usually involved too.process by which thestructures form is called protein folding and is a consequence of the primary structure. The mechanism of protein folding is not understood. Alhough polypeptide may have more than one stable folded conformation, each conformation has its own biological activity and only one conformation is considered to be the active, or native conformation.The two ends of the amino acid chain are referred to as the carboxy terminus and the amino terminus based on the nature of the free group on each extremity.

Functions
Proteins are involved in practically every function performed by a cell, including regulation of cellular functions such as signal transduction and metabolism. For example, catabolism requires enzymes termed proteases and other enzymes such as glycosidases.
Mechanisms of protein regulations molecules and ions are able to bind to specific sites on proteins. These sites are called binding sites. They exhibit chemical specificity. The particle that binds is called a ligand. The strength of ligand-protein binding is a property of the binding site known as affinity.Since proteins are involved in practically everyperformed by a cell, the mechanisms for controlling these functions therefore depend on controlling protein activity. Regulation can involve a protein's shape concentration. Some forms regulation include:Allosteric modulation: When the binding of a ligand at one site on a protein affects the binding of ligand at another site.
Covalent modulation: When the covalent modification of a protein affects the binding of a ligand or some other aspect of the protein's function.

Diversity
Proteins are generally large molecules, having molecular masses of up to 3,000,000 the muscle protein titin has a single amino acid chain 27,000 subunits long. Such long chains of amino acids are almost universally referred to as proteins, but shorter strings of amino acids are referred to as "polypeptides," "peptides" or rarely, "oligopeptides". The dividing line is undefined, though "polypeptide" usually refers to an amino acid chain lacking tertiary structure which may be erally classified as soluble, filamentous or membrane-associated Nearly all the biological catalysts known as enzymes are soluble proteins with a recent notable execption being the discovery of ribozymes, RNA molecules with the catalytic properties of enzymes Antibodies, the basis of the adaptive immune system, are another example of soluble proteins. Membrane-associated proteins include exchangers and ion channels, which move their substrates from place to place but do not change them; receptors, which do not modify their substrates but may simply shift shape upon binding them. Filamentous proteins make up the cytoskeleton of cells and much of the structure of animals: examples include tubulin, actin, collagen and keratin, all of which are important components of skin, , and cartilage. Another special class of proteins consists of motor proteins such as myosin, kinesin, and dynein. These proteins are "molecular motors," generating physical force which can move organelles, cells, and entire muscles.

Working with proteins
Proteins are sensitive to their environment. They may only be active in their native state, over a small pH range, and under solution conditions with a minimum quantity electrolytes. A protein in its native state is often described as folded. A proteinis not in its native state is said to be denatured. Denatured proteins generally have no well-defined secondary structure. Many proteins denature and will not remain in solution in distilled water.One of the more striking discoveries of the 20th century was that the native and denatured states in many proteins were interconvertible, that by careful control of solution conditionsdialyzing away a denaturing chemica, a denatured protein could be converted to native form. The issue of how proteins arrive at their native state is an important area of biochemical study, called the study of protein folding.

Through genetic engineering, researchers can alter the sequence and hence the structure, "targeting", susceptibility to regulation and other properties of a protein. The genetic sequences different proteins may be spliced together to create "chimeric" proteins that possess properties of both. This form of tinkering represents one of the chief tools of cell and molecular biologists change and to probe the workings of cells. Another area of protein research attempts to engineer proteins entirely new properties or functions, a field known as protein engineering.Protein-protein interactions can be screened for using two-hybrid screening.

structures are usually referred to as and transitions between them are called conformational changes.The primary structure is held together by covalent peptide bonds, which are made during the process of translation. The secondary structures are held together by hydrogen bonds. The tertiary structure is held together primarily by hydrophobic but hydrogen bonds, ionic interactions, and disulfide bonds are usually involved too.process by which thestructures form is called protein folding and is a consequence of the primary structure. The mechanism of protein folding is not understood. Alhough polypeptide may have more than one stable folded conformation, each conformation has its own biological activity and only one conformation is considered to be the active, or native conformation.The two ends of the amino acid chain are referred to as the carboxy terminus and the amino terminus based on the nature of the free group on each extremity.

Proteins are involved in practically every function performed by a cell, including regulation of cellular functions such as signal transduction and metabolism. For example, catabolism requires enzymes termed proteases and other enzymes such as glycosidases.
Mechanisms of protein regulations molecules and ions are able to bind to specific sites on proteins. These sites are called binding sites. They exhibit chemical specificity. The particle that binds is called a ligand. The strength of ligand-protein binding is a property of the binding site known as affinity.Since proteins are involved in practically everyperformed by a cell, the mechanisms for controlling these functions therefore depend on controlling protein activity. Regulation can involve a protein's shape concentration. Some forms regulation include:Allosteric modulation: When the binding of a ligand at one site on a protein affects the binding of ligand at another site.
Covalent modulation: When the covalent modification of a protein affects the binding of a ligand or some other aspect of the protein's function.

Proteins are generally large molecules, having molecular masses of up to 3,000,000 the muscle protein titin has a single amino acid chain 27,000 subunits long. Such long chains of amino acids are almost universally referred to as proteins, but shorter strings of amino acids are referred to as "polypeptides," "peptides" or rarely, "oligopeptides". The dividing line is undefined, though "polypeptide" usually refers to an amino acid chain lacking tertiary structure which may be erally classified as soluble, filamentous or membrane-associated Nearly all the biological catalysts known as enzymes are soluble proteins with a recent notable execption being the discovery of ribozymes, RNA molecules with the catalytic properties of enzymes Antibodies, the basis of the adaptive immune system, are another example of soluble proteins. Membrane-associated proteins include exchangers and ion channels, which move their substrates from place to place but do not change them; receptors, which do not modify their substrates but may simply shift shape upon binding them. Filamentous proteins make up the cytoskeleton of cells and much of the structure of animals: examples include tubulin, actin, collagen and keratin,In most jurisdictions (such as the United States), pharmacists are regulated separately from physicians. That is, the legislation stipulates that the practice of prescribing must be separate from the practice of dispensing. These jurisdictions also usually specify that only pharmacists may supply scheduled pharmaceuticals to the public, and that pharmacists cannot form business partnerships with physicians or give them "kickback" payments.

In the minority of jurisdictions , doctors are allowed to dispense drugs themselves and the practice of pharmacy is integrated with that of the physician.The reason for the majority rule is the high risk of a conflict of interest. Otherwise, the physician has a financial self-interest in "diagnosing" as many conditions as possible, and in exaggerating their seriousness, because he can then sell more medications to the patient. Such self-interest directly conflicts with the patient's interest in obtaining cost-effective medicatio
Community PharmacyA pharmacy commonly the chemist; or drugstore in the U.S.; or Apothecary, historically) is the place where most pharmacists practice the profession of pharmacy. It is community pharmacy where the dichotomy of the profession exists—health professionals who are also retailers.Community pharmacies usually consist of a retail storefront, with a dispensary where medications are stored and dispensed. The dispensary is subject to pharmacy legislation; with requirements for storage conditions, compulsory texts, equipment, etc., specified in legislation. Where it was once the case that pharmacists stayed within the dispensary compounded/dispensed medications; there has been an increasing trend towards the use of trained dispensary technicians while the pharmacist spends more time communicating with patients.here is a requirement that all pharmacies must have a pharmacist on-duty at all times it is open. In many jurisdictions it is also a requirement that the owner of a pharmacy must be a registered pharmacist. This latter requirement has been revoked in many jurisdictions, such that many retailers (including grocery stores and mass merchandisers) now include a pharmacy as department of their store

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