BIOMOLECULES
You have learnt in chemistry how elemental analysis is performed. If we perform such an analysis on a plant tissue, animal tissue or a microbial paste, we obtain a list of elements like carbon, hydrogen, oxygen and several others and their respective content per unit mass of a living tissue.
If the same analysis is performed on a piece of earth’s crust as an example of non-living matter, we obtain a similar list.
Biomolecules are divided into two types-inorganic and organic.
Inorganic biomolecules includes minerals, feasts and water and organic biomolecules includes carbohydrates, fats, proteins, nucleic acids, vitamins etc.
Different biomolecules can be classified as aldehyde, ketones and sweet composites as chemical form and amino acids, nucleotides and adipose acids as biochemical forms.
- Except lipids, macromolecules are formed by polymerization ofsub-units called monomers.
- Proteins are polymers of amino acids. Amino acids are linked by peptide bond formed by dehumidification between COOH group of one amino acids and NH3 group of coming with the junking of H2O.
- In nucleic acids, the phosphate motes links 3’C of sugar of one nucleoside to the 5’C of sugar of coming nucleosides releasing two water motes to form 3’-5’phosphodiester bond.
- In polysaccharides, the mono-saccharides are linked by glycosidic bonds formed by dehumidification between two carbon tittles of two conterminous monosaccharaides.
Carbohydrates (Polysaccharides)
Polysaccharides are long chain of sugar containing different monosaccharaides as a structure block.
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Proteins are polypeptide chains made up of amino acids. There are 20 types of amino acids joined together by peptide bond between amino and carboxylic group.
There are two kinds of amino acids.
a. Essential amino acids are attained by living organism along with food.
b. Unnecessary amino acids can be prepared by our body from raw accoutrements.
The main functions of protein in living cell are
a. Transport of nutrient across the membrane.
b. Fight contagious organisms.
c. Produce enzyme and proteins.
Collagen is the most abundant protein in beast world.
Primary structure of protein is the introductory structure of protein in which a number of polypeptides are involved having sequence of amino acids. The first amino acid of sequence is called N-terminal amino acids and last amino acid of peptide chain is called C-terminal amino acids.
Secondary structure proteins vestments forms helix. There are three types of secondary structure-α helix, β pleated and collagen. In α helix, the polypeptide chain is curled spirally in right handed manner.
In β pleated secondary proteins two of further polypeptide chains are connected by hydrogen bonds. In collagen there are three beaches or polypeptides curled around one another by hydrogen bonds.
In Tertiary structure long protein chain is folded upon itself like a concave woolen ball to give three dimensional view of protein.
(a) secondary structure (b) Tertiary structure
In Quaternary structure each polypeptide develops its own tertiary structure and function as subunit of protein.
Eg. Hemoglobin. In adult mortal hemoglobin 4sub-units are involved. The two subunits are of α type and two subunits of β types.
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Nucleic Acid
Nucleic acids are polynucleotides. A nucleic acid has three chemically distinct factors-heterocyclic emulsion (nitrogenous base), polysaccharides (ribose/ deoxy-ribose sugar) and phosphate or phosphoric acid.
CBSE Notes for Class 11 Biology
The sugar plant in nucleic acid is either ribose or deoxyribose. Nucleic acid containing deoxyribose sugar is called DNA (Deoxyribonucleic Acid) and those containing ribose sugars are called RNA (Ribonucleic acid).
Biomolecules are constantly being changed into some other biomolecules and also made from other biomolecules. This retardation and timber is through chemical process called metabolism.
In living organism, all the metabolic responses are enzyme catalyzed. Catalysts are those substances that alter the rate of response. The protein with catalytic power is called enzyme.
Biomolecules Class 11 Revision Notes
Metabolic Base for living organism
The metabolic pathways that lead to more complex structure from simpler structure are called biosynthetic or anabolic pathways and those pathways that lead to simpler structure from complex structure are called catabolic pathways.
Photosynthesis and protein conflation are illustration of anabolic and respiration and digestion are the illustration of catabolic pathways.
ATP (adenosine triphosphate) is the most important form of energy currency in living world.
All living organism live in steady state characterized by attention of each of the metabolites. The living state is anon-equilibrium steady state to be suitable to perform work.
Enzymes
Enzymes are generally proteinaceous substances which are able of catalyzing chemical responses of natural origin without themselves witnessing any change, generally called as biocatalysts.
The nucleic acids that bear like enzymes are called ribozymes.
The tertiary structure of protein has pockets or crack into which substrate fit to beget the biochemical responses.
The major difference between inorganic and organic catalyst is inorganic catalyst works effectively at high temperature and pressure but enzyme get damaged at high temperature.
The external energy needed to start a chemical response is called activation energy.
Factors impacting Enzyme Exertion
a. Temperature - An enzyme is active within a narrow range of temperature. Temperature ate which enzyme is most active is called optimum temperature. The enzyme exertion drop over and below this temperature.
b. pH – every enzymes has an optimum pH at which it's maximum active.Utmost of the intracellular enzymes work at neutral pH.
Attention of Substrate- increase in substrate attention increase the rate of response due to occupation of more active spots by substrate.
Competitive Asset-when the molecular structure of asset resembles the substrate that inhibits the function of enzymes.
Biomolecules Class 11 Revision Notes
Enzymes are classified as
(i) Oxidoreductases/ Dehydrogenases-
(ii) Transferases -
(iii) Hydrolases catalyzes the hydrolysis of peptide, ester, glycosidic bonds etc.
(iv) Lyases remove the groups from substrate.
(vi) Ligases – catalyzes the linking together of two composites.
Co-factors are the non-protein element of an enzyme to make the enzyme more catalytically more active. The protein portions of enzyme are called apoenzymes.
The essential chemical factors of any coenzymes are vitamins. As NAD and NADP contains vitamins niacin .