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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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