08/28/2017 Chapter 2

Monday, August 28, 2017

10:41 AM

Human Physiology
Nucleotides
-Consist of a phosphate group (could be more than one), five carbon sugar (e.g.
deoxyribose), nitrogenous base
-Function of single nucleotides
Capture and transfer energy in high energy electrons
NAD & FAD-electron carrier
-Cell to cell communication (e.g. cAMP )
Nucleic Acid
Store and transmit genetic information
Types of Bonds
Ionic-are strong electrostatic attraction between anion and cation

Hydrogen bonds-Weak attraction between hydrogen atom to nearby oxygen, nitrogen, and
fluoride. H-bonds are responsible for surface tensions.

Van Der Waals-weak attraction between the nucleus of any atoms and the electron of nearby
atoms.

Nonpolar and polar molecules

Ionic compounds are hydrophilic because the ions are going to form hydrogen bond with polar
water molecules.

Polar molecules are hydrophilic; unevenly shared bonding electrons; These molecule dissolve
easily in water
Nonpolar molecular-hydrophobic; do not dissolve well in water; must be carrier by a hydrophilic
molecule to carry into solution;

Protein can lose its native conformation by excess amount of ion disrupting the H-bonding

Molecular shape/function
Secondary-alpha helix and beta strand ; This is due to the bond angles between amino acid;
Beta-strand form sheets via hydrogen bond

Tertiary-globular and fibrous protein; This is due to non/covalent interactions (e.g. disulfide
bonds).

Free H+ ion can disrupt the conformation of a protein which may alter or destroy a function

Hydrogen ion
pH -a measure of the concentration of free H+ (acidity)

pH=-log[H+] with [H+] in mEq/L

 Acids-contribute H+ ion to the solution

Bases- Combine with the free H+ ions

Buffers-conjugated base or acids that moderate changes in pH

CO2 +H2OH2CO3H++HCO3-

If the blood become more acidic increases in H+ would lead to excess CO2

Ligands vs substrate

Ligand bind to any molecules

Substrate occurs when a molecule cause a reaction

All ligands are substrate but not all substrates are ligands

Protein binding reaction

Reversible, go to state of equilibrium and obey the law of mass action

Equilibrium constant represent binding affinity;
The higher the Keq, then [PL] is a favorable reaction

Kd=dissociation constant
A large Kd for a binding protein and its ligand means that the protein has a low affinity for
the ligand

Isoform have the similar function but have different affinity for ligands

Factor that influence Binding

May require proteolytic activity or cofactor
Antagonist are inhibitors that decrease activity of protein
Competitive inhibitor are reversible;

Allosteric inhibitors bind reversibly at remote regulatory sit

Covalent modulators- atoms or functional groups that bind covalently to protein and
alter the protein's property