Sunday, April 29, 2012

Key terms realated to Amino Acids (Glossary)

Amino acids : α-Amino-substituted carboxylic acids which is the building blocks of proteins.

R Groups : (1) Formally, an abbreviation denoting any alkyl group.
                  (2)Ocassionally, used in a more general sense to denote virtually any                                       organic substiuent (the R groups of amino acids, for example).

Chiral carbon : Carbon containing four different groups. Their mirror images do not superimpose with each other. This also known as assymetric carbon.

Chiral center : An atom with substiuents arranged so that the molecule is not superimposable on its mirror image.

Chiral compounds :  A compound that contains  an assymetric center (chiral atom or chiral center) and thus can occur in two nonsuperimposable mirror image forms (enantiomers).

Sterioisomers : Compounds that have the same composition and the same order of atomic connections but different molecular arrangements.

Enantiomers : Enantiomers are a special type of sterioisomers that are mirror images of each other  and the requires of a chiral carbon.

Optical Activity :  The capacity of a substance to rotate the plane of plane polarized light.

Levorotatory isomer :  Asterioisomer that rotates the plane  polarized light counterclockwise.

Dextrorotatory isomer :  A sterioisomer that rotates the plane polarized light clockwise.

D,L System : Nearly all biological compounds with a chiral center  occur naturally in only one sterioisomeric form either D or L. This is known as D,L, System.The amino acid residues in proteins are exclusively L-Sterioisomers.

RS System :  RS System is another system of specifying configuration around a chiral center used in the systematic nomenclature of organic chemistry and describes more precisely the configuration of molecules with more than one chiral center.

Absolute configuration :  The configuration of four different substiuent groups around an assymetric carbon atom, in relation to D- and L-glyceraldihyde.

Zwiter ion or dipolar ion :  Zwiterion(or dipolar ion) is a hybrid molecule containing positive and negative ionic groups . 

Isoelectric pH (Symbol pI) :  pI is defined as the pH at which a molecule exists as a zwiterion or dipolar ion and carries no net charge .Thus , the molecule is electrically neutral .











Saturday, April 28, 2012

BIOMOLECULES

Definition : An organic compound  those  normally present as an essential component of living organisms including large polymeric molecules such as pollysaccharide, proteins, lipids, nucleic acids as well as primary metabolites ,secondary metabolites  produced during various metabolic reaction and natural products.

There are many biomolecules but four classes of those namely  carbohydrates, proteins, lipids and nucleic acids  are essential;  present in all biological systems. This unit will cover the structure, reactivity, and properties  of organisms .

Types of Biomolecules :
  •  Small molecules :       
           * Lipids,Phospolipids, Glycolipids, sterol, Glycerolipids,Vitamins, Hormones,        Neurotransmeters,Metabolites.
  • Monomers,Oligomers and Polymers :
           * Monomers e.g. Amino acids, Monosaccharides, Isoprenem,neucleotides.

          *Oligomers e.g.Oligopeptides,oligosaccharides,terpenes, oligonucleotides.

          * Polymers e.g. polypeptide ,proteins (Hemoglobin) ; polysaccharides                     (Cellulose); Polyterpenes  Nucleic acids (DNA,RNA).


Other biomolecules besides the three essential biomolecules :

List of Biomolecules
A23187 (Calcimycin, Calcium Ionophore) Interferon
Abamectin Inulin
Abietic acid Ionomycin
Acetic acid Ionone
Acetylcholine Isoleucine
Actin Iron-sulfur cluster
Actinomycin D K252a
Adenosine K252b
Adenosine diphosphate (ADP) KT5720
Adenosine monophosphate (AMP) KT5823
Adenosine triphosphate (ATP) Keratin
Adenylate cyclase Kinase
Adonitol Lactase
Adrenaline, epinephrine Lactic acid
Adrenocorticotropic hormone (ACTH) Lactose
Aequorin Lanolin
Aflatoxin Lauric acid
Agar Leptin
Alamethicin Leptomycin B
Alanine Leucine
Albumins Lignin
Aldosterone Limonene
Aleurone Linalool
Alpha-amanitin Linoleic acid
Allantoin Linolenic acid
α-Amanatin, see Alpha-amanitin Lipase
Amino acid Lipid
Anabolic steroid Lipid anchored protein
Anethole Lipoamide
Angiotensinogen Lipoprotein
Amylase (also see α-amylase) Low density lipoprotein,LDL
Angiotensinogen Luteinizing hormone (LH)
Anisomycin Lycopene
Antidiuretic hormone (ADH) Lysine
Arabinose Lysozyme
Arginine Malic acid
Ascomycin Maltose
Ascorbic acid (vitamin C) Melatonin
Asparagine Membrane protein
Aspartic acid Metalloprotein
Asymmetric dimethylarginine Metallothionein
Atrial-natriuretic peptide (ANP) Methionine
Auxin Mimosine
Azadirachtin A – C35H44O16 Mithramycin A
Bacteriocin Mitomycin C
Beauvericin Monomer
Bicuculline Mycophenolic acid
Bilirubin Myoglobin
Biopolymer Myosin
Biotin (Vitamin H) Nucleic Acid
Brefeldin A Ochratoxin A
Brucine Oestrogens
Cadaverine Oligopeptide
Caffeine Oligomycin
Calciferol (Vitamin D) Orcin
calcitonin Orexin
Calmodulin Ornithine
Calmodulin Oxalic acid
Calreticulin Oxidase
Camphor Oxytocin
Cannabinol p53
Capsaicin PABA
Carbohydrase Paclitaxel
Carbohydrate Palmitic acid
Carnitine Pantothenic acid (Vitamin B5)
Carrageenan parathyroid hormone (PTH)
Casein Paraprotein
Caspase Pardaxin
Cellulase Parthenolide
Cellulose Patulin
Cerulenin Paxilline
Chelerythrine Penicillic acid
Chromomycin A3 Penicillin
Chaparonin Penitrem A
Chitin Peptidase
α-Chloralose Pepsin
Chlorophyll Peptide
Cholecystokinin (CCK) Peripheral membrane protein
Cholesterol Phenethylamine
Choline Phenylalanine
Chondroitin sulfate Phosphagen
Cinnamaldehyde phosphatase
Citral Phospholipid
Citric acid Phenylalanine
Citrinin Phytic acid
Citronellal Plant hormones
Citronellol Polypeptide
Citrulline Polyphenol
Cobalamin (Vitamin B12) Polysaccharide
Coenzyme Porphyrin
Coenzyme Q Prion
Colchicine Progesterone
Collagen Prolactin (PRL)
Coniine Proline
Corticosteroid Propionic acid
Corticosterone Protamine
Corticotropin-releasing hormone (CRH) Protease
Cortisol Protein
Creatine Proteinoid
Creatine kinase Putrescine
Crystallin Pyrethrin
α-Cyclodextrin Pyridoxine or pyridoxamine (Vitamin B6)
Cyclodextrin glycosyltransferase Pyrrolysine
Cyclopamine Pyruvic acid
Cyclopiazonic acid Quinone
Cysteine Radicicol
Cystine Raffinose
Cytidine Renin
Cytochalasin Retinene
Cytochalasin E Retinol (Vitamin A)
Cytochrome Rhodopsin (visual purple)
Cytochrome C Riboflavin (Vitamin B2)
Cytochrome c oxidase Ribofuranose, Ribose
Cytochrome c peroxidase Ricin
Cytokine RNA - Ribonucleic acid
Cytosine – C4H5N3O RuBisCO
Deoxycholic acid Safrole
DON (DeoxyNivalenol) Salicylaldehyde
Deoxyribofuranose Salicylic acid
Deoxyribose Salvinorin-A – C23H28O8
Deoxyribose nucleic acid (DNA) Saponin
Dextran Secretin
Dextrin Selenocysteine
DNA Selenomethionine
Dopamine Selenoprotein
Enzyme Serine
Ephedrine Serine kinase
Epinephrine – C9H13NO3 Serotonin
Erucic acid – CH3(CH2)7CH=CH(CH2)11COOH Skatole
Erythritol Signal recognition particle
Erythropoietin (EPO) Somatostatin
Estradiol Sorbic acid
Eugenol Squalene
Fatty acid Staurosporin
Fibrin Stearic acid
Fibronectin Sterigmatocystin
Folic acid (Vitamin M) Sterol
Follicle stimulating hormone (FSH) Strychnine
Formaldehyde Sucrose (sugar)
Formic acid Sugars (in general)
Forskolin superoxide
Fructose T2 Toxin
Fumonisin B1 Tannic acid
Gamma globulin Tannin
Galactose Tartaric acid
Gamma globulin Taurine
Gamma-aminobutyric acid Tetrodotoxin
Gamma-butyrolactone Thaumatin
Gamma-hydroxybutyrate (GHB) Topoisomerase
Gastrin Tyrosine kinase
Gelatin Taurine
Geraniol Testosterone
Globulin Tetrodotoxin
Glucagon Thapsigargin
Glucosamine Thaumatin
Glucose – C6H12O6 Thiamine (Vitamin B1) – C12H17ClN4OS·HCl
Glucose oxidase Threonine
Gluten Thrombopoietin
Glutamic acid Thymidine
Glutamine Thymine
Glutathione Thiamine (Vitamin B1)
Gluten Triacsin C
Glycerin (glycerol) Thyroid-stimulating hormone (TSH)
Glycine Thyrotropin-releasing hormone (TRH)
Glycogen Thyroxine (T4)
Glycolic acid Tocopherol (Vitamin E)
Glycoprotein Topoisomerase
Gonadotropin-releasing hormone (GnRH) Triiodothyronine (T3)
Granzyme Transmembrane receptor
Green fluorescent protein Trichostatin A
Growth hormone Trophic hormone
Growth hormone-releasing hormone (GHRH) Trypsin
GTPase Tryptophan
Guanine Tubulin
Guanosine Tunicamycin
Guanosine triphosphate (+GTP) Tyrosine
Haptoglobin Ubiquitin
Hematoxylin Uracil
Heme Urea
Hemerythrin Urease
Hemocyanin Uric acid – C5H4N4O3
Hemoglobin Uridine
Hemoprotein Valine
Heparan sulfate Valinomycin
High density lipoprotein, HDL Vanabins
Histamine Vasopressin
Histidine Verruculogen
Histone Vitamins (in general)
Histone methyltransferase Vitamin A (retinol)
HLA antigen Vitamin B ()
Homocysteine Vitamin B1 (thiamine)
Hormone Vitamin B2 (riboflavin)
human chorionic gonadotropin (hCG) Vitamin B3 (niacin or nicotinic acid)
Human growth hormone Vitamin B4 (adenine)
Hyaluronate Vitamin B5 (pantothenic acid)
Hyaluronidase Vitamin B6 (pyridoxine or pyridoxamine)
Hydrogen peroxide Vitamin B12 (cobalamin)
Hydroxyproline Vitamin C (ascorbic acid)
5-Hydroxytryptamine Vitamin D (calciferol)
Indigo Vitamin E (tocopherol)
Indole Vitamin F
Inosine Vitamin H (biotin)
Inositol Vitamin K (naphthoquinone)
Insulin Vitamin M (folic acid)
Insulin-like growth factor Vitamin P (niacin or nicotinic acid)
Integral membrane protein Water
Integrase Wortmannin
Integrin Xylose
Intein Zearalenone

Properties of biomolecules :
  •  Macromolecules and their Building blocks have a sense or directionality.
  •  Macromolecules are informational.
  •  Biomolecules have charateristic three-dimensional architechture.
  •  Weak forces maintain biological structure and determine biomolecular interactions .
Functions of four main biomolecules :
  1. Carbohydrates ( polymer of monosaccharides) : Storage of energy(as Glycogen), structures (building materials for cell walls ).
  2. Proteins (polymers of amino acids) : Realization of  the genetic information, catalytic and transport functions, building material,etc.
  3. Lipids(polymers of fatty acids) : Storage energy, structures(building material for cell membranes).
  4. Nucleic acids (polymers of nucleotides ( DNA and RNA) :



Wednesday, April 25, 2012

Amino Acids

Amino acids are a group of organic compounds  containing two functional groups--amino (-NH2) and carboxyl (-COOH).The Amino group is basic and the  carboxyl group is acidic in nature.These are structural unit of protein.Proteins are polymers of amino acids, with each amino acid residue joined to its neighbour by a specific type of covalent bond namely peptide bond that reflects the loss of the elements of water during joining of two amino acid.Proteins can be broken down( hydrolyzed) to their constituent amino acids by a variety of methods.

Atoms in amino acids structure : C,O,N,H and S.

General structure of Amino Acids :














Standard amino acids :

As many as 300 amino acids occure in nature, of these only 20 amino acids known as standard amino acids are repeatedly found in protein structure,isolated from different forms of life such animal,plant and microbial.The first to be discovered was asparagine, in 1806.The last of the 20 to be found,threonine, was not identified until 1938.

Structures of 20 standard amino acids :


Selenocystein - the 21 st amino acid : In recent years a 21 st amino acid namely selenocystein has been added.It is found in at the active sites of certain enzymes / proteins (selenoproteins), e.g. glutathione peroxidase,glycine reductase, thioredoxine reductase, 5'-deiodinase.

Pyrrolysine - in 2002 some researchers have described another amino acid namely pyrrolysine as the 22 nd amino acid. The stop codon UAG can code for pyrrolysine.

Non standard amino acids :

amino acids that have been chemically modified after they have been incorporated into a protein (termed a “posttranslational modification”) and those amino acids that occur in living organisms but are not found in proteins .Among these modified amino acids is γ-carboxyglutamic acid, a calcium-binding amino acid residue found in the blood-clotting protein prothrombin (as well as in other proteins that bind calcium as part of their biological function). The most abundant protein by mass in vertebrates is collagen. 
Some nonstandard amino acids are not found in proteins. Examples include lanthionine, 2-aminoisobutyric acid, dehydroalanine, and the neurotransmitter gamma-aminobutyric acid. Nonstandard amino acids often occur as intermediates in the metabolic pathways for standard amino acids — for example, ornithine and citrulline occur in the urea cycle, part of amino acid catabolism (see below). A rare exception to the dominance of α-amino acids in biology is the β-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B5), a component of coenzyme A.



Common structural features of amino acids :

1. All 20 of the common amino acids are a  α-amino acids.They have a carboxyl group and an amino group bonded to the same carbon atom (α carbon)
2. They differ from each other in their side chains , or R groups , which vary in structure, size, and electric charge , and which infuence the solubility of the amino acids in water.
3. The common amino acids of proteins have been assigned three-letter abbreviations and one-letter symbols,which are used as shorthand to indicate the composition and se quence of amino asids polymerized in proteins.
4. The additional carbons  in an R group are commonly designated β, γ, δ, ε and so forth proceeding out from the α carbon .
5. For most other organic molecules , carbon atoms are simply numbered from one end, giving highest priority(C-1) to the carbon with the substituent containing the atom of highest atomic number.Within  this lattter convention , the carboxylic carbon of an amino acid would be C-1 and the  α carbonwould be C-2 . Amino acids with heterocyclick R groups, the greek lettering system is ambigous and the numbering convention is therfore used.

   
        Lysin
6. The α carbon is known as chiral carbon (except glycine) because four different groups : a carboxylic group, an amine group, an R group, and a hydrogen bind to this carbon.
7. Amino acids have two possible sterioisomers because of the tetrahydral arrangement of bonding orbitals around the α-carbon atom. All molecules  with chiral center are also optically active i.e., they rotate plane -polarized light.

Classificattion of amino acids  :

There are different ways of classifying the amino acids based on the structure and chemical nature, nutritional requirement, metabolic fate etc.

A.Classification based on the structure :

1. Amino acids with aliphatic side chains : These are monoamino  monocarboxylic acids.The amino acids  of this class are glycine, alanine, valine, leucine, and isoleucine.The last three amino acids contain branched aliphatic side chains ,hence they are reffered to as branched chain amino acids.

2. Hydroxyl group containing amino acids: Serine, threonine,and tyrosine are hydroxyl group containing amino acids.

3. Sulfur containing amino acids : cysteine with sulfhydryl group and methionine with thioether group and cystine with two molecule of cystein joining by disulfied bond.

4. Acidic amino acids and their amides : Aspartic acid and glutamic acids  are dicarboxylic monoamino acids while asparagine and glutamine are their respective amide derivatives.

5. Basic amino acids : The three amino acids lysine , arginine(with guanido group) and histidine (with imidazole group) are monocarboxylic acids but basic in character.

6. Aromatic amino acids : Phenylalanine ,tyrosine,and tryptophan( with indole group) are aromatic amino acids.

7. Imino acids : proline containing pyrrolidine ring is a unique amino acid with an iminogroup(= NH).


B. Classification based on polarity :   Amino acids are classified into four groups based on their polarity.

1. Non-polar amino acids : These are hydrophobic ( water hating ).They have no charge in R group.The amino acids include in this class alanine, leucine,isoleucine ,valine , methionine, phenyl alanine tryptophan,and proline.

2. Polar amino  acids with no charge on R group :  The amino acids of this class do not carry charge on the R groups.They possege groups such as hydroxyl, sulfhydral , and amide .e.g. Glycine,serine, threonine, cystein,glutamine, asparagine and tyrosine.

3. Polar amino acids with positive R group : The three amino acids lysine ,arginine ,and histidine are included in this group.

4. Polar amino acids with negative R group : The dicarboxylic monoamino  acids- aspartic acid and glutamic acid are considered in this group.

C. Classification Based on Nutrition : The twenty common amino acids are classified into two classes based on their nutritional requirement those are required for the synthesis of variety of proteins and biological  functions.  

1. Essential or indispensable amino acids : The amino acids which cannot be synthesized by the body and therefore need to be supplied through the diet are called essential amino acids. They are required for proper growth and maintanence of the individual.The ten amino acids are essential for human :
Arginine, Valine, Histidin, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine,Threonine, Tryptophan.

Semi-essential amino acids : There are two amino acids namely Arginine and Histidine are partly synthesized by the adult body hence htey are known as semi essential amino acids.Thus 8 are absolutely essential while 2 are semi essential amino acids.

2. Non-essential or dispensable amino acids : The amino acids  which can be synthesized by the body to meet the biological needs known as non-essential amino acids. These are - Glycine, Alanine, Serine, Cystein, Asparagine, Aspartate, Glutamate, Glutamine,Tyrosine and proline.

D. Classification based on their metabolic fate : The carbon skeleton of amino acids cn serve as a precursor for the synthesis of glucose or fat or both. From metabolic view amino acids are divided into three classes :

1. Glycogenic amino acids :  the  amino acids which act as precursor of the glucose or glycogen biosynthesis e.g. Alanine, aspartate, glycine, methionine etc.

2. Ketogenic amino acids : the amino acids act as precursors for fat biosynthesis. Two amino acids are ketogenic leucine and lysine are exclusively ketogenic.

3. Glycogenic and Ketogenic amino acids : The four amino acids isoleucine, phenylalanine, tryptophan, tyrosine are precursors for the synthesis of glucose as well as fat.

Physiochemical propeties of Amino acids : 

A. Physical properties :

1. Solubility : Most of the amino acids are usually soluble in water and insoluble in  organic solvents .
2. Melting point : Amino acids are generally melt at higher temparatures, often avobe 200 degree centigrade.
3. Taste : Amino acids may be sweet (gly,ala,val), tasteless(leu), or bitter(Arg,Ile).
4. Optical properties : All the amino acids except glycine posseses optical isomers i.e.D-and L-Amino Acids due to the presence of asymmetric carbon atom. Some amino acids also have a second asymmetric carbon e.g. isoleucine,  threonine.
5. Amino acids as ampolytes : Amino acids contain both acidic (-COOH) and basic (-NH2) groups. They can donate a proton or accept a proton ,hence amino acids regarded as ampolytes.
6. Each Amino acids has characteristic pH (e.g. leucine  pH 6.0) at which it carries both positive and negative chargesand exsts as Zwitterion.
7. Amino acids have characteristic Titration curves.

B. Chemical properties :

1. The common chemical properties of all amino acids result from the presence of both α-carboxylic and α-amino groups in their molecules. The reactions connected with  specific features of the side chains allow to distinguish individual amino acids or some groups of amino acids.It refers to both free amino acids and those bound in peptide or protein molecules. Reaction with ninhydrin – a common reaction for all amino acids All amino acids and peptides, which contain a free α-amino group, react with ninhydrin forming a blue-violet product, whereas proline and hydroxyproline, which contain free imino groups, form a yellow product. During the ninhydrin reaction the amino acid undergoes decarboxylation and deamination. The released ammonia (NH3) binds to ninhydrin forming a blue-violet product. The reaction is presented on


 
Characteristic reactions for individual amino acids

2.The aromatic rings of phenylalanine, tyrosine and tryptophan submitted to the action of nitric acid (HNO3) form yellow nitroderivative products. This process is known as a xantoprotein reaction.
Tyrosine, like other phenols, reacts with Millon reagent, which is a mixture of mercury nitrates (V) and mercury nitrates (III) in nitric acid solution. The nitrophenols, resulting from the interaction of tyrosine with nitric acid (V) form red colour complexes with mercury. The heating of mixture containing free or peptide bound tyrosine with Millon reagent results in formation of red flocky sediment.

3.Sulphur-containing amino acids: cysteine and methionine – in strongly alkaline medium – are degraded releasing the sulphide ions (S2-), which react with lead (II) acetate forming brown-black lead (II) sulphide.
4. The guanidine group of arginine reacts with α-naphtol oxidised with bromate (I), releasing ammonia (NH3), and red colour complex.
5. The indol ring of tryptophan reacts with glyoxalic acid - in the presence of sulphuric (VI) acid - forming red-violet product. The glyoxalic acid exists as a contaminating component in commercial preparation of concentrated (glacial) acetic acid.
6. The imidazole ring of histidine, in the presence of sodium nitrite, reacts with sulphanilic acid forming yellow product.

Occurance and function in Biochemistry :

1.Amino acids are primary building  blocks of  various biologically active  proteins.

2.Amino acids can be metabolized to produce energy. This is especially
important during fasting, when the breakdown of muscle protein is a major
energy source.

3.Some amino acids act as neurotransmitters, and some act as starting
materials for the biosynthesis of neurotransmitters, hormones, and other
important biochemical compounds.

Amino acids useful as drugs :

There are certain non-standard amino acids that are used as drugs .
  • D-peniciline (D- dimethylglycine), a metabolite of peniciline is employed in the chelation therapy of Willson's disease.
  • N-Acetylcysteine is used in cystic fibrosis and chrionic renal insufficiency ,as it can function as an antioxidant.
  • Gabapentin (γ- aminobutyrate linked to cytohexane) is used as an anticonvulsant.


Sources and biological function of  amino acids.







Saturday, April 14, 2012

Biochemistry and its scope

Introduction

Biochemistry is the study of chemistry of  biological system i.e. biochemistry is the branch of life science in which discuss the various chemical substance and chemical reaction occuring in living organisms.Life is chemical process which  is directed by thousands of enzymatic reactions in an organized manner.These enzymatic reactions occuring in living organisms are known as metabolic reactions.The term Biochemistry was first introduced by the German Chemist Carl Neuberg in 1903.

The study of  Biochemistry takes into account the studies related to the nature of the chemical constituents of living matter, their transformations in biological systems and the energy changes associated with these transformations. 

Modern Biochemistry has two Branches, Descriptive Biochemistry  and Dynamic Biochemistry.

Descriptive Biochemistry : This branch deals with the qualitative and quantitative characterization of various living components.
Dynamic Biochemistry : This branch deals with the  elucidation of the nature and the mecahnism of the bichemical reaction occuring in living cell in organisms.

Many effective disciplines have been emerged from biochemistry such as Enzymology (Study of enzymes),Endocrionology (Study of hormones),Clinical Biochemistry (Study of diseases),Molecular biochemistry (Study of biomolecules) etc.Along with these discipline some other modern branch are developed to fill requirement of developmental world e.g. Agriculture Biochemistry, Pharmacological Biochemistry etc.

Peoples those acquire a sound knowledge of Biochemistry can take two step concerns in Biomedical science.

1 . Understand and maintain health
2 . understand and treatment of diseases

History of  Biochemistry

(Proteins - enzymes)
1828 Wohler --> synthesized a biological compound (urea) from ammonium cyanate (an inorganic chemical)! NH4+ NCO-

1833  the Anselme Payen discover first enzyme diastase (today called Amylase)

1897 the Buchner brothers (Eduard and Hans) demonstrated that alcoholic fermentation could occur in a cell-free extract.

1926 J.B. Sumner demonstrated that an enzyme (urease) was a protein and could be crystallized (indicative of fixed molecular structure and purity)

1950s  James D. Watson, Francis Crick, Rosalind Franklin, and Maurice Wilkins were instrumental in solving DNA structure and suggesting its relationship with genetic transfer of information.

1958, George Beadle and Edward Tatum received the Nobel Prize for work in fungi showing that onegene produces one enzyme.

1988, Colin Pitchfork was the first person convicted of murder with DNA evidence, which led to growth of forensic science.

2006 Andrew Z. Fire and Craig C. Mello received the  Nobel Prize for discovering the role of RNA interference (RNAi), in the silencing of gene expression.

Scopes and jobs of Biochemistry

There are various feilds  in which a Biochemist find employment  and apply their acquired knowledge include:

Private Sector:
  • Biotechnology
  • Chemical manufacturing companies
  • Food and Drink (includes brewing)
  • Health and Beauty Care
  • Medical Instrument companies
  • Research Companies and Laboratories
Public Sectors:
  • Agriculture and fisheries
  • Blood Service
  • Cancer research institutes
  • Environmental Pollution Control
  • Forensic Science
  • Hospitals
  • National Blood Services
  • Overseas Development
  • Public Health Entities
  • Public Health Laboratories
  • Pharmaceutical firms
  • Food industry andagrochemical companies
Institutes of research as employ students of Biochemistry. Educational institutions also take in professionals in the field of Biochemistry.

Job profiles:
  • Biologist
  • Biomedical Scientist
  • Biotechnologist
  • Chemical Examiners
  • Chemist
  • Clinical Scientist
  • Food Scientist
  • Forensic Scientist
  • Laboratory Technician
  • Microbiologist
  • Pharmacologist
  • Research Associates
  • Research Officers
  • Research Scientist
  • Quality control analyst

Objectives of Biochemists

The major objective of  a Biochemist is the complete understanding of all the chemical processes associated with living cells at the molecular level. To achieve this objective, biochemists have attempted to isolate numerous molecules (bio molecules).

In brief the objectives can be listed as follows:

1. Isolation, structural elucidation and the determination of mode of action of biomolecules.
2. Identification of disease mechanisms.
3. Study of in born errors of metabolism
4. Study of oncogenes in cancer cells
5. The relationship of biochemistry with genetics, physiology, immunology, pharmacology, toxicology etc. 

Biochemistry is related to almost all the life sciences and without biochemistry background and knowledge, a thorough understanding of health and well-being is not possible.