NEET MDS Lessons
Biochemistry
IONIZATION OF WATER, WEAK ACIDS AND WEAK BASES
The ionization of water can be described by an equilibrium constant. When weak acids or weak bases are dissolved in water, they can contribute H+ by ionizing (if acids) or consume H+ by being protonated (if bases). These processes are also governed by equilibrium constants
Water molecules have a slight tendency to undergo reversible ionization to yield a hydrogen ion and a hydroxide ion :
H2O = H+ + OH−
The position of equilibrium of any chemical reaction is given by its equilibrium constant. For the general reaction,
A+B = C + D
3-D Structure of proteins
Proteins are the main players in the life of a cell. Each protein is a unique sequence of amino acid residues, each of which folds into a unique, stable, three dimentional structure that is biologically functional.
Conformation = spatial arrangement of atoms that depends on rotation of bonds. Can change without breaking covalent bonds.
- Since each residue has a number of possible conformations, and there are many residues in a protein, the number of possible conformations for a protein is enormous.
Native conformation = single, stable shape a protein assumes under physiological conditions.
- In native conformation, rotation around covalent bonds in polypeptide is constrained by a number of factors ( H-bonding, weak interactions, steric interference)
- Biological function of proteins depends completely on its conformation. In biology, shape is everything.
- Proteins can be classified as globular or fibrous.
There are 4 levels of protein structure
- Primary structure
- linear sequence of amino acids
- held by covalent forces
- primary structure determines all oversall shape of folded polypeptides (i.e primary structure determines secondary , tertiary, and quaternary structures)
- Secondary structure
- regions of regularly repeating conformations of the peptide chain (α helices, β sheets)
- maintained by H-bonds between amide hydrogens and carbonyl oxygens of peptide backbone.
- Tertiary structure
- completely folded and compacted polypeptide chain.
- stabilized by interactions of sidechains of non-neighboring amino acid residues (fibrous proteins lack tertiary structure)
- Quaternary structure
- association of two or more polypeptide chains into a multisubunit protein.
Vitamin B12: Cobalamin
Vitamin B12, also known as cobalamin, aids in the building of genetic material, production of normal red blood cells, and maintenance of the nervous system.
RDA The Recommended Dietary Allowance (RDA) for vitamin B12 is 2.4 mcg/day for adult males and females
Vitamin B12 Deficiency
Vitamin B12 deficiency most commonly affects strict vegetarians (those who eat no animal products), infants of vegan mothers, and the elderly. Symptoms of deficiency include anemia, fatigue, neurological disorders, and degeneration of nerves resulting in numbness and tingling.
By rearranging the above equation we arrive at the Henderson-Hasselbalch equation:
pH = pKa + log[A-]/[HA]
It should be obvious now that the pH of a solution of any acid (for which the equilibrium constant is known, and there are numerous tables with this information) can be calculated knowing the concentration of the acid, HA, and its conjugate base [A-].
At the point of the dissociation where the concentration of the conjugate base [A-] = to that of the acid [HA]:
pH = pKa + log[1]
The log of 1 = 0. Thus, at the mid-point of a titration of a weak acid:
pKa = pH
In other words, the term pKa is that pH at which an equivalent distribution of acid and conjugate base (or base and conjugate acid) exists in solution.
Biotin
Biotin helps release energy from carbohydrates and aids in the metabolism of fats, proteins and carbohydrates from food.
RDA The Adequate Intake (AI) for Biotin is 30 mcg/day for adult males and females
Biotin Deficiency Biotin deficiency is uncommon under normal circumstances, but symptoms include fatigue, loss of appetite, nausea, vomiting, depression, muscle pains, heart abnormalities and anemia.
Titration of a weak acid with a strong base
• A weak acid is mostly in its conjugate acid form
• When strong base is added, it removes protons from the solution, more and more acid is in the conjugate base form, and the pH increases
• When the moles of base added equals half the total moles of acid, the weak acid and its conjugate base are in equal amounts. The ratio of CB / WA = 1 and according to the HH equation, pH = pKa + log(1) or pH = pKa.
• If more base is added, the conjugate base form becomes greater till the equivalance point when all of the acid is in the conjugate base form.
The amino acids buffer system
Amino acids contain in their molecule both an acidic (− COOH) and a basic (− NH2) group. They can be visualized as existing in the form of a neutral zwitterion in which a hydrogen atom can pass between the carboxyl and amino groups.
By the addition or subtraction of a hydrogen ion to or from the zwitterion, either the cation or anion form will be produced
Thus, when OH− ions are added to the solution of amino acid, they take up H+ from it to form water, and the anion is produced. If H+ ions are added, they are taken up by the zwitterion to produce the cation form. In practice, if NaOH is added, the salt H2N - CH2 - COONa would be formed. and the addition of HCl would result in the formation of amino acid hydrochloride.