Welcome to:. Biochemistry-I. Dr. Moayad H. Khataibeh Head, Department of Pharmacology College of Pharmacy Alkharj University. PHL 213 = Biochemistry-I, 2 (2+0).
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The course deals with the following topics in biochemistry: amino acids and proteins including enzymes, biological oxidation, porphyrins and nucleic acids. The effects of certain xenobiotics (foreign chemicals) including drugs and toxic agents on molecular level and the basis of their clinical impact are emphasized whenever possible.
There are four major noncovalent forces involved in the structure and function of biomolecules:
i) hydrogen bonds
More important when they occur between and within molecules --> stabilize structures such as proteins and nucleic acids.
ii) hydrophobic interactions
Important in protein shape and membrane structure.
iii) charge-charge interactions or (ionic bonds)
Occur between two oppositely charged particles.
Strongest noncovalent force that occurs over greater distances.
Can be weakened significantly by water molecules (can interfere with bonding).
iv)van der Waals forces
e.g. protein ------> amino acids
2H2O ---> H3O+ + OH-, but usually written
H2O ---> H+ + OH-
Keq = [H+][OH-]
1.0 x 10-14M2 = [H+]2
1.0 x 10-7 = [H+]
pH= - log [H+], so at equilibrium
e.g. HCl ---> H+ + Cl-
weak acid (H) ----> H+ + A-
Ka = [H+] [conjugate base or A-]
blood plasma-carbon dioxide- carbonic acid- bicarbonate buffer system
CO2 + H2O ----> H2CO3 -------> HCO3- + H+
If [H+] increases (pH falls), momentary increase in [H2CO3], and equation goes to the left.