The basic principles underlying the innovative technique of noninvasive biomolecular manipulation using hydrosomes can be understood only if we acquire a clear idea about the molecular fundamentals of vital activity and pathology in the living organism. This can be achieved by an overall study of structure of important chemical compounds that make up part of living matter, their transformation and physico-chemical properties that constitute the basis of vital activity.

Such a study comprises the structural and functional interrelationships and conversions of chemical compounds in the organism, the routes of energy transformation in the living systems, the regulatory mechanisms of chemical conversions and physico-chemical processes in the cells, the molecular mechanism of transfer of genetic information etc. For the limited purpose of explaining the basic principles of Hydrosome therapy, let us confine ourselves to a study of structural and functional properties of proteins, the most important class of biological molecules associated with the phenomenon of life.

Proteins- molecular carriers of life: -
A general understanding of the molecular interactions that constitute life is invariably associated with the study of proteins (from Greek word Proteios, which means Primary), the major cell components of any living organism. Proteins play many vitally important roles in all biological processes. They never occur in inorganic nature. Hence the saying: “‘there is no Life without Proteins; there is no Proteins without Life”. Proteins may be called the molecular carriers of life.

Proteins are high molecular, nitrogen containing organic compounds with very complex structural organization. Proteins are polymers of amino acid molecules linked into chains by a special kind of chemical bonding called peptide bonds. There are about twenty different types of amino acids known to exist, which combine in a variety of ways, thereby deriving about to 1012 types of diverse protein molecules. Information regarding the synthesis of each type of protein molecule is encoded in small specific submits of chromosomes, called gene. Proteins are synthesized from amino acid molecules, according to the plan provided by concerned gene, through the mediation of RNA and a number of specific enzymes. Each type of protein molecule is intended to play a particular role in the living organism. Proteins play a wide range of roles in biological processes, the specificity of which are determined by the high level of structural organization of protein molecules.

It is only the proper spatial arrangement that render the protein active; otherwise, any disorganization of its spatial structure produces alterations in its properties, and may lead to a loss of biological activity. This decisive role of spatial organization of proteins is of paramount importance in the mechanism of vital activity and pathology. Any mechanism that induces a change in the three dimensional tertiary configuration of a particular protein molecule, invariably leads to some break in the continuity of the biochemical channel, of which the protein forms parts of, resulting in a pathologic condition.

Biological functions of proteins span such a wide spectrum of activity in the living organism, that it becomes quite a problem to name biological processes that should not involve proteins. No biological activity of any kind exists without an involvement of some protein molecules of one or other kind. Even in the genetic functions, which is commonly considered to be outside the protein competence and comes within the jurisdiction of nucleic acids, the role of protein is very important in the form of enzymes that control and mediate the expression of genetic functions of DNA.

Biological functions of proteins can be briefly summarized as follows: -
(a) Enzymatic catalytic function: -
This is a very common and most essential protein function, accelerating or facilitating chemical conversions in the organism. This includes synthesis and degradation of materials, transfer of electrons, atoms and molecules from one compound to another etc. E.g. (a) Fumarate hydratase, which catalyzes the reversible conversion of Fumarate+H2O ----- maleate. (2) Cytochrome oxydase, which participate in the transfer of electrons on to oxygen. (A detailed study of enzymes is given in the following part of this article)

(b) Hormonal or Regulatory Function: -
Proteins of this category play a role in the regulation of intracellular metabolism throughout the whole organism. E.g. (1) Insulin, which participate in the regulation of metabolic processes involving carbohydrates, proteins, fats, and other materials (2) Lutropin, which participate in the regulation of progesterone synthesis in the ovarian corpus leutium.

(c) Receptory Function: -
This class of receptor proteins participates in the selective binding of various regulators (hormones, mediators and cyclic nucleotides) on the surface of the cell membranes or inside the cells (cytosolic receptors). E.g. (1) Cytosolic receptor of estradiol, which binds estradiol inside the cells of for example, those of endometrium. (2) Glucagon receptor, which binds the hormone glucogon on to the surface of cell membrane, for example, that of liver. (3) Regulator subunit of protein kinase, which binds c AMP inside the cells.

(d) Transport function: -
This function of protein is expressed by binding and transporting of materials between tissues and through the cell membranes. E.g.. (1) Lipoproteins, which are responsible for the transport and distribution of the lipids in the tissues of organism. (2) Transcortin, which is responsible for transport of cortico steroids (hormones secreted by adrenal cortex into the blood). (3) Myoglobin, which is responsible for transport of oxygen in the muscle cells.

e) Structural, Supportive and Mechanical Functions: - Proteins play a structural role by their involvement in the build up of various membranes. E.g. (1) structural proteins of mitochondria, cytoplasmic membranes etc.

(2) Collagen, which is the structural element of supporting framework of osseous tissues, tendons and skin. (3) Fibroin, which participate in the formation of silkworm cocoon capsule. (4) B-Keratin, which is the structural basis for wool, nail and hoof.

f) Reserve or Trophic Function: -
Proteins are utilized as reserve materials for nutrition of developing cells. Eg. (1) Prolamines and glutelins which are reserve materials in wheat grain. (2) Ovalbumin, which is the reserve proteins of hen’s egg.

(g) Substrate- Energetic Function:-
This function is very close to trophic function. Protein is used as a substrate for energy supply. On degradation, one gram of protein releases 17.1 KJ of energy. Eg. All proteins ( dietary or intra cellular) decomposes into end products releasing energy.

(h) Mechano- Chemical Function:-
Some proteins plays a role in the movment of organism by contractions, using chemical energy. E.g. (1) myosin, which are fixed filaments in myofibrils.(2) actin, which are movable filaments in myofibrils.

(i) Electro- Osmotic function:-
Some proteins are involved in the build up of electric charge difference (Eletro Chemical gradient) and ion concentration gradient across cell membrane. E.g:-Na+ K+ ATP ase, is an enzyme mediating in the build up of Na+ K+ ion concentration gradient and electro chemical gradient across the cell membranes.

(j) Energy Converting Function:-
These proteins are involved in the conversion of electronic and osmotic energy into chemical energy. E.g. (1) ATP- synthetase, which performs the synthesis of ATP owing to the electro potential difference or ion osmotic concentration gradient across the cell membrane.

(k) Co- genetic Function:-
Even though proteins themselves are not genetic (hereditary) material, they assist the nucleic acids in the accomplishment of self reproduction and genetic information transfer. In the absence of appropriate proteins, nucleic acids are incapable of expressing their genetic function. E.g.(1) DNA polymerase is an enzyme participating in the replication of DNA.(2) DNA dependent RNA polymerase is an enzyme involved in the information transfer from DNA to RNA.

(l) Gene-Regulatory Function:-
Certain proteins participate in the regulation of template functions of nuceicacids and genetic information transfer. E.g. (1) Histones are proteins participating in the regulation of replication and, in part, of transcription of certain portions of DNA. (2) Acidic proteins participate in the regulation of transcription of certain portions of DNA.

(m) Immunologic or Anti toxic Functions:-
Antibodies, which are protein molecules, participate in the defence reactions against foreign antigens and micro organisms ( toxins produced by them ) via formation of antigen-antibody complexes. E.g. (1) Immune globulins IgA, IgM, IgG etc. perform defence functions. (1) Compliment proteins, which are a complex series of enzymatic proteins, interact to combine with antigen-antibody complexes.

(n) Detoxicating Functions:-
Proteins, owing to their functional groups, are capable of binding toxic compounds (heavymetal ions and alkaloids ) rendering them harmless to the organism. E.g. Albumins can act as binding agents for heavy metals and alkaloids.

(o) Toxigenic Functions:-
Certain proteins and peptides produced by organism (primarily micro organisms) are poisionous for other living organisms. E.g. Botulinus Toxin, which is secreted by Bacillus Botulinses.

(p) Haemostatic Functions:-
These proteins participates in the thrombosis and arrest bleeding. Eg. Fibrinogen, is a protein in blood serum which can polymerize as a network and act as structural network for thromb formation.

From the above discussions, the decisive role played by proteins as the major participant of biological functions is self explanatory. The mode and mechanism of functioning of protein molecules can be clearly understood from a detailed study of enzymes, which are the major components of total proteins in the living organism. A clear understanding of the molecular mechanisms of protein interactions is necessary to explain the basic principles of hydrosome therapy. Enzymes may be considered as the perfect models for the study of structural and functional mechanisms of proteins.

ENZYMES

All the chemical processes in the living organism can proceed only with the involvement of enzymes. Enzymes are biological catalysts of protein nature, very superior in catalytic activity to that of non enzymatic catalysts. The rate of enzyme catalysis is very high. A single enzyme molecule can, at normal body temperature (370C) catalyze about 103 to 106 molecules per minute. Such high rates are unimaginable in nonenzymatic catalysis. Another peculiarity of enzymes is their high specificity, which enables them to direct metabolic processes to strictly defined channels. There are enzymes that act selectively on only one stereoisomer of a compound. Enzymes, being protein molecules, are susceptible to temperature variations, and to changes in medium pH. At present, it is believed that the cell contains about 104 enzyme molecules, capable of catalysing over 2000 various reactions. There are about 1800 types of specific enzymes known yet. About 150 enzymes have been isolated in crystalline form.

Structural and Functional Organisation of Enzymes:-
The enzymes exhibit all features characteristic of structural organisation of protein molecules. As any other protein, they possess four levels of organisation: Primary, secondary, tertiary and quarternary. The enzymes with quarternary structures are composed of protomers(sub units) and constitute a preponderant type. Similar to other functional proteins, there are simple enzyme proteins and conjugated enzyme proteins. A conjugated enzyme is composed of a protein portion called apoenzyme, and a nonprotein portion called co-factor. The co-factor in enzymes are metal ions or co-enzymes. Co-enzymes are small organic molecules attached to the apoenzymes. Apoenzymes and co-enzymes join together to form a conjugated protein enzyme molecule called Holoenzyme.

Functional Organisation of Enzymes:-
In the three dimensional structure of a simple, as well as conjugated, enzyme, there are distinguished a number of specific regions responsible for certain specific functions. A portion of enzyme molecule constitutes the active centre, which is the site in the enzyme spatial structure where the binding with a substrate take place. ( Substrate is a compound that undergoes conversion by the action of enzyme). This active centre may be schematically depicted as a recess or pocket, for the sake of convenience. The active centre of conjugated enzymes include co-factors. The number of active centres on specific enzyme molecule may vary. Along side of the active centre, an enzyme has a regulatory or allosteric centre, spatially remote from the active centre of the molecule. The name allosteric centre implies that the molecules bound to this centre are structurally dissimilar from the substrate, but exert influences on the binding and conversion of the substrate at the active centre, by changing the substrate configuration. One enzyme molecule can have more than one allosteric centres. Compounds capable of binding to the allosteric centres are called allosteric effectors. They exert influence, through the allosteric centre, on the function of active centres, in a facilitating or inhibiting manner. Accordingly, allosteric effectors are reffered to as possitive( activators) or negative (inhibitor) regulators of enzymes.

In the active centre of enzymes, there are anchor sites for binding substrates, and catalytic sites, where conversion of bound substrates takes place. There are also some accessory groups and facilitating groups, which play specific roles in binding the substrates to active centres. The actual catalytic and contact are assigned to special functional groups, which are actually the side chain radicals of amino acids contained in the protein molecules. Any agent that can block these functional groups impede the activity of enzymes.

Co-factors play a very important role in the functioning of enzyme molecules. As stated previously, they are metal ions or co-ezymes. Co-factors are either tightly bound to enzyme active centre , susceptible to easy cleavage by dialysis. The term prosthetic group is applied to tightly bound co-factors. Occasionally, it is difficult to differentiate between the co-enzyme and the substrate, since a co-enzyme bound substrate can be liable to attack by the enzymes. In such cases, the co-enzyme can be considered as a co-substrate.

Co-enzymes are broadly classified in to :-
(1) Vitamin co-enzymes and (2) Non vitamin co-enzymes
Vitamin co-enzymes consist of (a) Thiamine co-enzymes (TMP,TDP and TTPO (b) Flavin co-enzymes (FMN &FAD) (c) Pantothenic co-enzymes( CoA,Diphospho CoA,4-Phospho panthothenate) (d) Nicotonamide co-enzymes(NAD& NADP) (e) pyridoxine co-enzymes(PALP&PAMP) (f) Folic co-enzymes (THFA), (g) cobamide co-enzymes(Methyl cobalamine and deoxy adenosyl cobalamine) (h) Biotin coenzymes (carboxy biotin) (i) Lipotic coenzymes (Lipo amide) (j) Quinone coenzymes(abiquinone and plastiquinone)and (k)Carnitine co-enzymes (Carnitine).

Non vitamic co-enzymes are (a) Nucleotide co-enzymes,(b) Monosacharide phosphates (c) Metaloporphyrin co-enzymes and (d) Peptide co-enzymes.

Vitamins are parent materials for various co-enzymes of first group. Therefore their dietary deficiency affects the synthesis of co-enzymes, which leads to an impaired functioning of corresponding conjugated enzymes. Metal ions are likewise capable of acting as co-factors for certain enzymes. Such enzymes are called metallo enzymes. Iron, copper, molybdinum, cobalt, zinc, magnesium, mangenese and calcium are commonly found as co-factors. This shows their importance in the biological activities of living organisms. It should be borne in mind that metals, similar to vitamin co-enzymes are supplied to the organism through food. Therefore, the normal functioning of a large number of enzymes is dependent on a regular supply of metals, most of which fall in to the group of microelements. This explains the high biological activity of metals. Their dietary deficiency may lead to grave metabolic disturbances in the organism.

Mechanism of Enzyme Action:
The enzyme organisation, complicated both from structural and functional standpoints, provides to certain extent a clue to a deeper understanding of their characteristic features, which are high specificity and high catalysis rate. The process of enzyme catalysis may conventionally be differentiated in to three steps.(a) Diffusion of a substrate to an enzyme, resulting in a stereospecific binding of the former to the active site of enzyme, there by forming an enzyme-substrate complex.(b) Conversion of the primary enzyme -substrate complex in to one or more activated enzyme-substrate complexes.(c) Detachment of reaction products from the active centre of enzymes and their diffusion in to the environment.

Enzymes exhibit a varying degree of specificity towards substrates. Some enzymes catalyses conversion of only one among all possible substrate stereoisomers. For example, the enzyme fumarate hydratase catalyses the conversion of only fumaric acid, and never of its stereoisomer, maleic acid. On the other hand, some enzymes are specific to a single substrate only, whereas certain other enzymes catalyses conversion of a related groups of substrates. There are some broad spectrum enzymes such as cytochrom P 450 which participates in the catalysis of a large number of compounds.

How can the specific action of an enzyme be explained? This mechanism of enzyme specificity is found in other types of proteins also, engaged in diverse non-enzymic functions in the living organism. There have been proposed two hypotheses concerning this intriguing problem. The first one is that put forward by Fischer, known as ‘key and lock’ hypothesis. It states that the enzymic specificity lies in a strict conformity of substrate with the active centre of enzyme. According to Fischer, the enzyme is a rigid structure, whose active centre is a replica of the substrate. The enzyme action is feasible if the substrate matches the active centre as the key fits the lock. If the substrate (key) becomes slightly modified, it no longer fits the active centre (lock) and no reaction takes place. The fischer hypothesis is rather attractive since it provides a simple explanation of the specificity if the enzyme action. However, adhering to the ‘key and lock’ hypothesis, one would hesitate explicitly, for example, the absolute and relative group substrate specificity, in view of a large variety of ‘key’(substrate) configuration that fit the ‘lock’ (enzyme).

Another hypothesis that has been suggested by Coshland appears to circumvent the above apparent discrepencies. This hypothesis is commonly referred to as ‘the induced fit model’. According to coshland hypothesis, the molecule of an enzyme is a flexible,elastic rather than rigid, structure (this is borne out by the available experimental evidence). The conformation of an enzyme or its active centre is subject to alteration on addition of a substrate or any other ligand. More over, the active centre is not a rigid replica of the substrate, and the latter enforces upon the active centre to adopt an appropriate form at the onset of addition (hence the name ‘induced fit model’). In other words, the coshland ‘lock’ is made up of a pliable material and, therefore, is capable of adopting on configuration appropriate to the ‘key’on enzyme-substrat contact.

The ‘induced fit model’ hypothesis has been corroborated by experimental evidence. It has been ascertained that, in a number of enzymes, an arrangement of functional groups of the active centre is changed after substrate addition. Within the framework of this model, it is also possible to explain the difference in conversion of closely related substrate analogues. If a ‘false’substrate(pseudo substrate) differs from the ‘true’ (native) substrate in minor details, and the active centre of enzyme adopts a conformation close to the true one, the arrangement of catalytic groups in such an enzyme-substrate complex enables the reaction to be carried out. The enzyme, figuratively speaking, seems to disregard this ‘mystification’. But the enzyme reaction will proceed at a slower rate as compared with the authentic substrate, since in the former case, no perfect match for the catalytic groups in the enzyme active centre has been achieved. No reaction will take place, if the quasi substrate nconfiguration precludes an appropriate accommodation of the catalytic groups, apparently, the varied extent of conformational reorganisation of active centre. If the range is limited to a single feasible conformation, the enzyme is highly specific. If the possibility of active centre rearrangement spans a wilder range, the enzyme can respond to quasi-substrates as well. Any substance, that can bind to the active centre of enzymes by virtue of their spatial configuration, without engaging in enzymic conversions, act as inhibitors of the particular enzyme, there by resulting in a pathologic condition

Regulation of Enzymic Activity:-
As has already been emphasised, the enzymes are catalysts with controlled activity. Therefore, the rates of chemical reactions in the organism can be monitored through the intermediacy of enzymes. The regulation of enzymic activity can be effected through the interaction of enzymes with various biological components or foreign compounds (pharmaceuticals, toxins etc.) which are commonly called enzyme modifiers or enzyme regulators. The modifiers that are capable, by their action on enzymes, of accelerating the reactions are called activators; if the modifiers retard the reactions, they are referred to as inhibitors.

The activation of an enzyme is defined by the acceleration of enzymic action after the onset of modifier action. Some activators are compounds effecting the active centre region of enzyme. This group of activators include substrates and enzyme co-factors. The co-factors (metal ions and coenzymes), while being essential structural elements of conjugated enzymes, are actually acting as activators to the enzyme molecules. As activators, metal ions exhibit a very specific behavior. Some of the enzymes need several, rather than one, metal ions for normal functioning. For example, Na+ K+-ATPase, which is responsible for the transport of monovalent cations across the cell membrane, requires magnesium, sodium and pottassium ions as activators. The activation by metal ions is effected by a variety of mechanisms. The specific involvement of co-enzymes in binding and catalysing the substrate account for their role as the activators. Some activators act by binding to allosteric centre of enzyme molecules. In such cases they are called allosteric activators.

Inhibition of enzymes are of special interest for an understanding of the mechanism of enzyme catalysis. A study of various agents capable of binding to the functional groups of contact and catalytic sites of enzyme active centres enables one to elucidate the importance of different groups involved in catalysis. Inhibitors provide a clue to the rationalisation of enzymic catalysis and can also be employed as a tool in studying the role of separate chemical reactions that may be specifically switched off by means of appropriate inhibitor for the given enzyme. The investigation of enzymic inhibitory reaction is important from the stand point of practical applications for the synthesis of medicinal drugs, pesticides etc and in elucidation of the mechanism of their actions.

A certain degree of caution should be exercised in employing the term inhibitor. The mere fact of a retardation of enzymic reaction does not warrant that we have observed an inhibitory effect. Any denaturants can suppress the enzymic reaction. Such a suppression may be called inactivation, rather than inhibition. Occasionally, situations may arise when a compound taken in small amounts acts as an inhibitor,and, taken in large amounts,as an inactivator. Therefore the differentiation between inhibitor and inactivator appears to be somewhat arbitrary.

The common feature of all inhibitors is their ability of binding to the enzyme molecules. Viewed in this light, the inhibitors can be divided into two groups:reversible and irreversible inhibitors. Irreversible inhibitors are tightly bound to enzyme molecules, and hence the activity of enzyme cannot be restored by ordinary type of dialysis or dilution. On the contrary, the complex formed by enzyme and a reversible inhibitor is unstable and is liable to an easy dissociation, which results in the restoration of enzymic activity.

According to the mechanism of their action, the enzyme inhibitors are subdivided into following major types: (1) competitive inhibitors (2) Non-competitive inhibitors (3) uncompetitive inhibitors (4) substrate linked inhibitors and (5) allosteric inhibitors.

Competitive Inhibition of Enzymes:-
This is the retardation of enzymic reaction produced by binding the enzyme active centre with an inhibitor structurally related to the substrate and capable of preventing the formation of enzyme-substrate complex. Under competitive inhibition conditions, the inhibitor and the substrate, being structurally related species,compete for the active centre of enzyme. The competing compound present in excess, binds preferably to the active centre of the enzyme. The enzyme becomes bound in such a way that an enzyme-inhibitor complex is formed. This kind of inhibition occurs as substrate-like inhibitory agents bind a certain number of enzyme molecules,rendering the latter incapable of forming an enzyme-substrate complex. The removal of the inhibitory blocking can be accomplished by an excess of substrate, whose molecules eliminate the inhibitors from the active centre of enzyme molecules and reactivate the latter to catalytic activity. Because of the resemblance between the competitive inhibitor and the substrate, this type of inhibition is also called isosteric inhibition. The function of a competitive inhibitor can also be exercised by metabolites as well as foreign compounds that enter the body. The action of numerous pharmaceuticals and pesticides,as well as various warfare gases, is based on the principle of competitive inhibition.

By selectively switching off various enzymes,one may perform a survey of functions of enzymes in the process of metabolism. The study of competitive inhibitors offers ample scope for a search for anti-metabolites which, while exhibiting configurationally resemblance with authentic substrates,may fall into the category of competitive inhibitors. Anti-metabolites are promising for use as specific pharmaceuticals.However,it should be kept in mind that competitive relations are possible not only between the substrate and inhibitor, but also between inhibitor and coenzymes, until coenzymes (analogues of coenzymes, incapable of enzymic activity) likewise act as competitive inhibitors by putting out of action the enzyme molecules to which they are bound. Anti co-enzymes (or their precursers,antivitamins) are widely used in bio-chemical studies and medical practice as effective drugs.

Non-competitive inhibition of Enzymes:
It is the retardation associated with the effect of an inhibitor on the catalytic convertion,rather than on the substrate-enzyme binding. A non-competitive inhibitor either directly binds to the catalytic groups of enzyme active centre or,on binding with the enzyme,leaves the active centre free and induces conformational changes in it. The conformational changes affect the structure of catalytic site and hinder its interaction with substrate.Since the non-competitive inhibitor exhibits no effect on the substrate binding in this case, as distinct from competitive inhibition,a substrate-enzyme complex is formed. But this does not lead to any conversion reactions. A classical example of non-competitive inhibition is cynide poisoning. Cynides are capable of strongly binding with the trivalent iron forming part of the catalytic moiety of hemin enzyme, cytochrome oxidase, there by putting off the respiratory chain leading to the death of cells. Heavy metal ions and their organic compounds belong to non-competitive inhibitors of enzymes. For this reason, ions of heavy metals (‘mercury,lead, cadmium,arsenic and some others) are very toxic. Distinct from competitive inhibitors,eliminating the non-competitive inhibitors is rather difficult. De-blocking can be accomplished only through the agency of inhibitor-binding compounds called –reactivators . Heavy metals act as non-competitive inhibitors only when taken in small concentrations. Taken in excess, they act as inactivators or denaturants. Non-competitive inhibitors are employed as pharmaceutical drugs, pesticides,as well as for military purposes. Intoxication with heavy metals can be removed by the elimination of toxins by binding with reactivators or antidotes.

Un-competitive inhibition:-
This is the retardation of enzymic action produced by addition of an inhibitor to an enzyme-substrate complex only. An un-competitive inhibitor does not bind to the enzyme in the absence of a substrate. Moreover , the inhibitor facilitates the addition of substrate, and then, on binding with the latter, inibits the enzyme. This kind of inhibition is less common than those discussed above.

Substrate linked Inhibition:-
It is the retardation of enzymic reaction produced by a substrate taken in excess. This type of inhibition occurs due to the formation of an enzyme-substrate complex in a way that the enzymatic conversion of the substrate is not possible. Figuratively, it may be described as an overcrowding of substrate molecules, thereby resulting in enzyme inhibition

Role of molecular regulation mechanism in vital activity and pathology

Structure and mechanism of interactions (including regulatory mechanism) discussed above with regard to the enzymes is also broadly applicable to other types of proteins, which play diverse role in the living organism. The mechanism of molecular binding, activation and inhibition also operates in receptors, transporters and other types of protein molecules. The role of spacial configuration of specific protein molecules in ensuring the unimpaired functioning of vital activity is explicit. The normal maintenance of life processes basically depends upon the the unhindered functioning of diverse protein molecules engaged in different biological activities. As we all know, there is not a single biological activity unconnected with the involvement of some or other types of protein molecules. Hence, any deviation from the normal functioning of vital processes is invariably associated with some or other molecular errors related to proteins. Any factor (exogenous of endogenous ) that negatively interferes in the normal interactions of protein molecules may lead to a condition of pathology. Since the ability of a protein to play a particular role in the biological processes is determined by its specific spacial configuration arising from its three dimensional tertiary structure, any configurational deviation of the protein may lead to its inactivation. Such a condition renders the protein incapable of playing the specific biological role assigned to it. The molecular error results in a break in the continuity of the biochemical channels mediated by that particular protein, which amounts to a condition of pathology.

Molecular errors of proteins (or, proteinopathies) are mainly of two kinds. (a)Genetic (b) Acquired. Genetic proteinopathy is that condition of protein molecular error, which arises from a faulty synthesis of particular types of protein. This condition may be hereditory, where the genetic disposition is carried over from previous generation. The error may be caused by the mutation of genetic materials due to the effect of some mutagenic agents. Error in protein synthesis may also be the result of other proteinopathies associated with the mediatory proteins (enzymes) involved in protein synthesis. This indicates the possibility of chain effects of proteinopathies. Deficient protein synthesis may also be caused by a deficiency of supply of necessary building materials (aminoacids, co-factors etc). Acquired proteinopathies are protein errors arising after normal synthesis of a particular protein. This type of protein errors originates from secondary changes in molecular configurations arising from some external influences. These external factors may be (a) Inhibitory or (b) Enviornmental. Inhibitory proteinopathies are caused by the binding of some foreign molecules or ions {endogenous or exogenous) on the protein molecule (on active sites or allosteric sites), thereby changing its configurational pattern, rendering it unfit for specific biological functions. Enviornmental factors resulting in protein molecular errors are the changes in the microenviornment of the organism such as temperature, pH etc. Such factors also renders the protein molecules incapable of normal functioning, through configurational changes.

References :
Principle of Molecular imprinting technology
A way to make artificial locks for molecular keys By Ol of Ramstrom
Pure and Applied Biochemistry