Biomolecules are biological molecules i.e. which are present in the living organisms. Bio molecules includes macromolecules like DNA, RNA, carbohydrates nucleic acid and small molecules like ATP, NADPH, etc. Biomolecules are "molecules of life" however they are life less but, in appropriate complexity and number, molecules compose of living things. ATP and NADPH are energized biomolecules because they represent chemically useful forms of stored energy.
Most biomolecules are made up of just four atoms-oxygen, hydrogen, carbon and nitrogen however the different composition of these atoms gives diversity to biomolecules.
Biomolecules are those molecules which are present exclusively in the living organisms. They are formed in the body to manage the needs of physiology and growth. They maintain the life of organism. Some bio molecules are hereditary like DNA and transfer from organism to their of springs and some are structural component of the cell like proteins. They involve in all type of physiologically process.
Biochemistry is branch of science that deals with the formation of biomolecules, their role in the cell. It also describes how biomolecules regulate and maintain the life and any deficiency diseases. The biomolecules are present in the body of humans, animals and plants. Phototrophs (plant) Synthesised complex bio molecules take glucose from simplest carbon source (CO2). Plants pass their biomolecues to animal through food chain and food web. Animals convert the complex bio molecules into simple biomolecules and derive the energy from complex biomolecules. A biomolecule i.e. involved in the maintenance and metabolic process of living organisms.
1.1 Types of biomolecules
These 4 major biomolecules include
2. Proteins (amino-acids)
3. Fats (Lipids)
4. Nucleic acids (DNA, RNA, nucleotide).
2. CHEMICAL BONDING
It is an interaction between molecules. All five macromolecules interact with each other for example protein interact with DNA, Protein interact with RNA etc. The interaction is of two type
1. Covalent bonding
2. Non covalent bonding
2.1. Covalent bond
It is a chemical bond that involves the sharing of electrons between atoms. This is the strongest force. It is the bond which hold the atoms together. A typical carbon-carbon (C-C) covalent bond has a bond length of 1.54 Å and bond energy of 85 kcal mol-1 (356 kJ mol-1).
Example of covalent bond
Non polar covalent bond is chemical bond in which two atoms share a pair of electron with each other.
eg.-Non polar covalent bond is found in methane (CH4). The Lewis structure shows the electrons which is shared between C and H atoms.
Polar covalent bonding is a chemical bond where a pair of electron is equally shared between two atoms. It has significant ionic character. It means that the two shared electrons are closer to one of the atoms than the other, creating an imbalance of charge.
eg. Polar covalent bond is water (H2O)
2.2 Non covalent bonding
Non covalent bonds do not involve staring of electrons between atom like in covalent bond. It is a bond that is found between two macromolecules
It is a reversible interactions of biomolecules. Four types of noncovalent bonds are formed between macro molecules. The four fundamental noncovalent bonds are electrostatic interactions, hydrogen bonds, hydrophobic bond and vanderwaals interactions. They differ in geometry, strength, and specificity. These bonds are greatly affected in different manner in the presence of water.
2.2.1. Electrostatic interactions
An electrostatic interaction depends on the electric charges on atoms. An ionic bond is a type of chemical bond formed through an electrostatic attraction between two oppositely charged ions. Ionic bond are formed due to the transfer of electron from one donor atom to another acceptor atom like sodium atom to fluorine. In general, electrostatic interaction takes place between two stationary charges. The energy of an electrostatic interaction is given by Coulomb's law:
where E is the energy, q1 and q2 are the charges on the two atoms (in units of the electronic charge), r is the distance between the two atoms (in angstroms) and k is a constant.
2.2.2 Hydrogen bonds
Four conditions needs to be fulfilled for hydrogen bonding
1. Hydrogen is must for hydrogen bonding
2. The hydrogen must be sandwich between
two highly electronegative atom
3. The distance between the electro negative
atom and hydrogen must be 2.8 A°
4. The bond must be in plane.
Hydrogen bonds are relatively weak interactions, which are crucial for biological macromolecules such as DNA and proteins. The solubility of any molecule in water is also dependent upon hydrogen bonding. Hydrogen bonds are fundamentally electrostatic interactions. Normally hydrogen bonding is formed by fluorine, oxygen and nitrogen. The electronegative atom (like F, O, N) to which the hydrogen atom is covalently bonded pulls shared electron density away from the hydrogen atom because of this the hydrogen develops a partial positive charge (+) and the electronegative atom develops partial negative charge (–). Thus, the covalently bonded hydrogen of one molecule can interact with an other atom having a partial negative charge (–) through an electrostatic interaction.
The large difference in electronegativities between hydrogen and any of fluorine, nitrogen and oxygen, coupled with their lone pairs of electrons cause strong electrostatic forces between molecules. Hydrogen bonds are responsible for the high boiling points of water and ammonia with respect to their heavier analogues.
2.2.3. Van der Waals interactions.
The basis of Van der Waals interaction is that the distribution of electronic charge around an atom changes with time. The distribution changes with time is because of movement of electrons in the orbit. Electron is not a static, it revolves around the orbit.
Due to the movement of electron at any instant, the charge distribution is not perfectly symmetric. This transient asymmetry in the electronic charge around an atom acts through electrostatic interactions to induce a complementary asymmetry in the electron distribution around its neighboring atoms.
The resulting attraction between two atoms increases as they come closer to each other. The minimum distance between the molecule is known as vanderwalls contact distance. At a shorter distance, very strong repulsive forces become dominant because the outer electron clouds overlap to each other. Thus atoms repel to each other. That's the reason vanderwalls forces is the sum of attractive and repulsive forces.
Three types of Van der Walls forces
1. Dipole - Dipole
2. Dipole - induced Dipole
3. London - forces
London dispersion force :
A type of Van der Walls force is known as London dispersion force. The London dispersion force arises due to instantaneous dipoles in neighbouring atoms. As the negative charge of the electron is not uniform around the whole atom, there is always a charge imbalance. This small charge will induce a corresponding dipole in a nearby molecule; causing an attraction between the two. The electron then moves to another part of the electron cloud and the attraction is broken. London dispersion force is the weakest intermolecular force. London dispersive force is a temporary attractive force that results when electrons in two atom occupy positions that make the atoms form temporary dipoles. This force is also known as induced-dipole-induced dipole attraction.
2.2.4. Hydrophobic interaction
Hydrophobic force is not a force, is an interaction of non polar molecules like lipids which come close to each other only in presence of water. The hydrophobic force is a tendency of water molecules to form a bigger cage around the lipid molecules. The hydrophobic force does not exist without water. It is a tendency of water molecule only. Hydrophobic are generally non polar molecules and have long chain of carbon molecule which do not interact with water molecules.