BIOMOLECULES CHEMISTRY ASSIGNMENT

March 1, 2018 | Author: Amarendra Shukla | Category: Biomolecules, Macromolecules, Proteins, Dna, Rna
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BIOMOLECULES...

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Chemistry assignment TOPIC :

BIOMOLECULES

“THERE ARE AS MANY ATOMS IN A SINGLE AMOLECULE OF A DNA AS THERE ARE STARS IN A TYPICAL GALAXY.WE ARE ,EACH OF US,A LITTLE UNIVERSE “

BY: AMARENDRA P SHUKLA ROLL NO: 3 CLASS: XI SCIENCE

CONTENTS 1. CERTIFICATE 2. ACKNOWLEDGEMENT 3. BIOMOLECULES 4. TYPES OF BIOMOLECULES 4.1 MICROMOLECULES 4.1.1. AMINO ACID 4.1.2. SUGAR 4.1.3. LIPID 4.1.4. NUCLEOTIDES

4.2. MACROMOLECULES 4.2.1. POLYSACCARIDES 4.2.2. NUCLEIC ACID 4.2.3. PROTEINS

5.MONOMERS 6.METABOLIC BASIS FOR LIVING 7.THE LIVING STATE 8.IMPORTANT QUESTION AND CONCEPT OF BIOMOLECULES

CERTIFICATE THIS IS TO CERTIFY MASTER AMARENDRA P SHUKLA A STUDENT OF CLASS XI SCIENCE HAS SUCCESFULLY COMPLETED THE RESEARCH PROJECT ON THE TOPIC BIOMOLECULES UNDER THE GUIDANCE OF MRS SAPNA SINGH DURING THE ACADEMIC YEAR 2017-2018

PRINCIPAL

TEACHER

EXTERNAL

IN CHARGE

IN CHARGE

ACKNOWLEDGEMENT I WANT TO EXPRESS MY SINCERE THANKS TO MY RESPECTED PRINCIPAL MADAM AND CHEMISTRY TEACHER MRS SAPNA SINGH FOR GIVING ME A CHANCE TO RESEARCH ON THE TOPIC BIOMOLECULES AND IT HAS BEEN MY PLEASURE DOING SO .THIS HAS ADDED MANY POINTS TO MY KNOWLEDGE ABOUT CHEMISTRY AND ITS PRACTICAL APPLICATION .I ALSO THANK THEM FOR THEIR SUPPORT AND VALUABLE GUIDANCE WHICH HAS SEEEMED GREAT CONTRIBUTION IN COMPLETION OF MY RESEARCH WORK AS A PROJECT.

A biomolecule or biological molecule is a loosely used term for molecules or more commonly ions that are present in organisms. Biomolecules including large macromolecules (or polyanions) such as proteins, carbohydrates, lipids,and nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites, and natural products.

Biology and its subsets of biochemistry and molecular biology study biomolecules and their reactions. Most biomolecules are organic compounds, and just four elements—oxygen, carbon, hydrogen, and nitrogen—make up 96% of the human body's mass. But many other elements, such as the various biometals, are present in small amounts.

TYPES OF BIOMOLECULES MICRO MOLECULES BIOMOLECULES MACROMOLECULES M < 1000

MICROMOLECULE

AMONIO ACID SUGARS LIPIDS NUCLEOTIDES

M>1000

MACROMOLECULE

POLYSACCARIDES NUCLEIC ACID PROTEINS

MICROMOLECULE

Amino acid contain both amino and carboxylic acid functional groups. (In biochemistry, the term amino acid is used when referring to those amino acids in which the amino and carboxylate functionalities are attached to the same carbon, plus proline which is not actually an amino acid). Modified amino acids are sometimes observed in proteins; this is usually the result of enzymatic modification after translation (protein synthesis). For example, phosphorylation of serine by kinases and dephosphorylation by phosphatases is an important control mechanism in the cell cycle. Only two amino acids other than the standard twenty are known to be incorporated into proteins during translation, in certain organisms:

Selenocysteine is incorporated into some proteins at a UGA codon, which is normally a stop codon.  Pyrrolysine is incorporated into some proteins at a UAG codon. For instance, in some methanogens in enzymes that are used to produce methane. Besides those used in protein synthesis, other biologically important amino acids include carnitine (used in lipid transport within a cell), ornithine, GABA and taurine. 

AROMATIC AMONIO ACID

MONOSHACCARIDES: Simplest sugar,which cannot ne hydrolysed further into smaller sugars      

Composed of 3-7 C atoms: Triose (3C) Tetrose (4C) Pentose (5C) Hexose (6C) Heptose (7C) GLUCOSE:

GLACTOSE:

For lipids present in biological membranes, the Lipids (oleaginous) are chiefly fatty acid esters, and are the basic building blocks of biological membranes. Another biological role is energy storage (e.g., triglycerides). Most lipids consist of a polar or hydrophilic head (typically glycerol) and one to three nonpolar or hydrophobic fatty acid tails, and therefore they are amphiphilic. Fatty acids consist of unbranched chains of carbon atoms that are connected by single bonds alone (saturated fatty acids) or by both single and double bonds (unsaturated fatty acids). The chains are usually 14-24 carbon groups long, but it is always an even number. hydrophilic head is from one of three classes:  Glycolipids, whose heads contain an oligosaccharide with 1-15 saccharide residues.  Phospholipids, whose heads contain a positively charged group that is linked to the tail by a negatively charged phosphate group.  Sterols, whose heads contain a planar steroid ring, for example, cholesterol. Other lipids include prostaglandins and leukotrienes which are both 20-carbon fatty acyl units synthesized from arachidonic acid. They are also known as fatty acids

Nucleotides are organic molecules that serve as the monomer units for forming the nucleic acid polymers deoxyribonucleic acid (DNA) and ribonucleic acid(RNA), both of which are essential biomolecules in all life-forms on Earth. Nucleotides are the building blocks of nucleic acids; they are composed of three subunit molecules: a nitrogenous base a five-carbon sugar (ribose or deoxyribose), and at least one phosphate group. They are also known as phosphatenucleotides. A nucleoside is a nitrogenous base and a 5-carbon sugar. Thus a nucleoside plus a phosphate group yields a nucleotide. Nucleotides also play a central role in life-form metabolism at the fundamental, cellular level. They carry packets of chemical energy—in the form of the nucleoside triphosphates ATP, GTP, CTP and UTP—throughout the cell to the many cellular functions that demand energy, which include synthesizing amino acids, proteins and cell membranes and parts; moving the cell and moving cell parts, both internally and intercellularly; dividing the cell.

Purine + pyridimine

monomers

Higher nucleotides store energy in their higher energy P bond Nicotinamide + riboplavin coenzymes Coenzymes: non protein organic moiety of holoenzymes

MACROMOLECULE Polysaccharides are polymerized monosaccharides, or complex carbohydrates. They have multiple simple sugars. Examples are starch, cellulose, and glycogen. They are generally large and often have a complex branched connectivity. Because of their size, polysaccharides are not water-soluble, but their many hydroxy groups become hydrated individually when exposed to water, and some polysaccharides form thick colloidal dispersions when heated in water. Shorter polysaccharides, with 3 - 10 monomers, are called oligosaccharides .A fluorescent indicatordisplacement molecular imprinting sensor was developed for discriminating saccharides. It successfully discriminated three brands of orange juice beverage. The change in fluorescence intensity of the sensing films resulting is directly related to the saccharide concentration.

Nucleic acids are biopolymers, or large biomolecules, essential to all known forms of life. They are composed of monomers, which are nucleotides made of three components: a 5-carbon sugar, a phosphate group and a nitrogenous base. If the sugar is a simple ribose, the polymer is RNA (ribonucleic acid); if the sugar is derived from ribose as deoxyribose, the polymer is DNA (deoxyribonucleic acid). Nucleic acids are the most important of all biomolecules. They are found in abundance in all living things, where they function to create and encode and then store information in the nucleus of every living cell of every life-form organism on Earth. In turn, they function to transmit and express that information inside and outside the cell nucleus—to the interior operations of the cell and ultimately to the next generation of each living organism. The encoded information is contained and conveyed via the nucleic acid sequence, which provides the 'ladder-step' ordering of nucleotides within the molecules of RNA and DNA.

DNA structure is dominated by the wellknown double helix formed by Watson-Crick basepairing of C with G and A with T. This is known as Bform DNA, and is overwhelmingly the most favourable and common state of DNA; its highly specific and stable base-pairing is the basis of reliable genetic information storage. DNA can sometimes occur as single strands (often needing to be stabilized by single-strand binding proteins) or as A-form or Zform helices, and occasionally in more complex 3D structures such as the crossover at Holliday junctions during DNA replication.

Stereo 3D image of a group I intron ribozyme gray lines show base pairs; ribbon arrows show double-helix regions, blue to red from 5' to 3' end; white ribbon is an RNA product. RNA, in contrast, forms large and complex 3D tertiary structures reminiscent of proteins, as well as the loose single strands with locally folded regions that constitute messenger RNA molecules. Those RNA structures contain many stretches of A-form double

helix, connected into definite 3D arrangements by single-stranded loops, bulges, and junctions. Examples are RNA, ribosomes, ribozymes, and riboswitches. These complex structures are facilitated by the fact that RNA backbone has less local flexibility than DNA but a large set of distinct conformations, apparently because of both positive and negative interactions of the extra OH on the ribose. Structured RNA molecules can do highly specific binding of other molecules and can themselves be recognized specifically; in addition, they can perform enzymatic catalysis (when they are known as "ribozymes", as initially discovered by Tom Cech and colleagues.

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific threedimensional structure that determines its activity.

STRUCTURE OF PROTEIN The particular series of amino acids that form a protein is known as that protein's primary structure. This sequence is determined by the genetic makeup of the individual. It specifies the order of side-chain groups along the linear polypeptide "backbone". Proteins have two types of well-classified, frequently occurring elements of local structure defined by a particular pattern of hydrogen bonds along the backbone: alpha helix and beta sheet. Their number and arrangement is called the secondary structure of the protein. Alpha helices are regular spirals stabilized by hydrogen bonds between the backbone CO group (carbonyl) of one amino acid residue and the backbone NH group (amide) of the i+4 residue. The

spiral has about 3.6 amino acids per turn, and the amino acid side chains stick out from the cylinder of the helix. Beta pleated sheets are formed by backbone hydrogen bonds between individual beta strands each of which is in an "extended", or fully stretched-out, conformation.

When two or more polypeptide chains (either of identical or of different sequence) cluster to form a protein, quaternary structure of protein is formed. Quaternary structure is an attribute of polymeric (same-sequence chains) or heteromeric (different-sequence chains) proteins like hemoglobin, which consists of two "alpha" and two "beta" polypeptide chains.

Apoenzymes An apoenzyme (or, generally, an apoprotein) is the protein without any small-molecule cofactors, substrates, or inhibitors bound. It is often important as an inactive storage, transport, or secretory form of a protein. This is required, for instance, to protect the secretory cell from the activity of that protein. Apoenzymes becomes active enzymes on addition of a cofactor. Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds, (e.g., flavin and heme). Organic cofactors can be either prosthetic groups, which are tightly bound to an enzyme, or coenzymes, which are released from the enzyme's active site during the reaction.

Isoenzymes Isoenzymes, or isozymes, are multiple forms of an enzyme, with slightly different protein sequence and closely similar but usually not identical functions. They are either products of different genes, or else different products of alternative splicing. They may either be produced in different organs or cell types to perform the same function, or several isoenzymes may be produced in the same cell type under differential regulation to suit the needs of changing development or environment. The relative levels of isoenzymes in blood can be used to diagnose problems in the organ of secretion.

MONOMERS A monomer is a molecule that, as a unit, binds chemically or supramolecularly to other molecules to form a supramolecular polymer. Large numbers of monomer units combine to form polymers in a process called polymerization. Molecules of a small number of monomer units (up to a few dozen) are called oligomers. The term "monomeric protein" may also be used to describe one of the proteins making up a multiprotein complex. Biopolymer groupings, and the types of monomers that create them. 







For lipids (Diglycerides, triglycerides), the monomers are glycerol and fatty acids. For proteins (Polypeptides), the monomers are amino acids. For Nucleic acids (DNA/RNA), the monomers are nucleotides, each of which is made of a pentose sugar, a nitrogenous base and a phosphate group. For carbohydrates (Polysaccharides specifically and disaccharides—depends), the monomers are monosaccharides.

Metabolic pathways can lead to a more complex structure from a simpler structure (for example, acetic acid becomes cholesterol) or lead to a simpler structure from a complex structure (for example, glucose becomes lactic acid in our skeletal muscle). The former cases are called biosynthetic pathways or anabolic pathways. The latter constitute degradation and hence are called catabolic pathways. Anabolic pathways, as expected, consume energy. Assembly of a protein from amino acids requires energy input. On the other hand, catabolic pathways lead to the release of energy. For example, when glucose is degraded to lactic acid in our skeletal muscle, energy is liberated. This metabolic pathway from glucose to lactic acid which occurs in 10 metabolic steps is called glycolysis. Living organisms have learnt to trap this energy liberated during degradation and store it in the form of chemical bonds. As and when needed, this bond energy is utilized for biosynthetic, osmotic and mechanical work that we perform. The most important form of energy currency in living systems is the bond energy in a chemical called adenosine triphosphate (ATP).

 Thousand of chemical compound in a living organism, otherwise called metabolities or biomolecules are present at concentration characterstics of each of them. For example the blood concentration of glucose in a normal healthy individual is 4.5-5.0 mm while that hormone would be nanograms/ml  The most important fact of biological system is that all living organism exist in a steady-stale characterised by concentration of each of these molecule  These biomolecules are in metabolic flux  Any chemical or physical process move simultaneously to equilibrium. The steady state is non-equlibrium state . one should remember from the physics that system at equilibrium cannot perform work. As living organisms work continuously ,they cannot afford to each equilibrium. Hence the living state is the nonequlibrium sready state to be able to perform work; living process is a constant effort to prevent falling into equilibrium. This is achieved by energy input.  Metabolism provide a mechanismfor the production of the energy. Hence the living state and metabolism are synonomus. Without metabolism there cannot be living state.

QUESTION 1 – Why are biomolecules essential to life? ANSWERBiomolecules are organic molecules especially macromolecules like carbohydrates, proteins in living organisms. All living forms bacteria, algae, plant and animals are made of similar macromolecules that are responsible for life. All the carbon compounds we get from living tissues can be called biomolecules. QUESTION 2What is the structure of a biomolecule? ANSWERBiomolecular structure is the intricate folded, threedimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. QUESTION 3What is the function of a biomolecule? ANSWERProteins make up the majority of biomolecules present in a cell. These molecules have enormous variation. Proteins are responsible for many enzymatic functions in the cell

and play an important structural role . Proteins are composed of subunits called amino acids . QUESTIONS 4What is the purpose of biomolecules? ANSWER Proteins carry out specific functions inside cells, and they act as enzymes to catalyze reactions all over the body. ... Proteins are typically large molecules that can be built up from chains of amino acids called polypeptides. Nucleic acids are central to the function of living cells. QUESTION 5What are the biomolecules made of? ANSWER Biomolecules are made of building-block monomers. A monomer is a small molecule that can be combined chemically with other monomers to form larger molecules. Monomers are made up of relatively simple elements. The most abundant elements in biological monomers are carbon, hydrogen, and oxygen QUESTION 6Why biological molecules are important? ANSWERMost biological molecules have a core made of carbon and hydrogen. Molecules differ in structure and function, in part, because of different functional groups. The major classes of biological molecules that are important for all living things are carbohydrates, lipids, proteins, and nucleic acids.

QUESTION 7Is water a biomolecule? ANSWERA biomolecule is a chemical compound that naturally occurs in living organisms. ... As clear from above, the essential constituent of bio-molecules are carbon and hydrogen, and water does not contain carbon ,hence, it can not be considered as a bio-molecule. QUESTION 8What type of biomolecule is an enzyme? ANSWEREnzymes are usually proteins, and they act as catalysts for reactions. The proteins vary from enzyme to enzyme, depending on the location and function. They are always in globular form, to allow for easy accommodation for the substrate and active sites.

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