Pharmaceutical Biochemistry: Prelim

Antoine Lavoiser

Proposed that the combustion of a candle is similar to the respiration of animals, as both need Oxygen.

Vitalism

A common belief; compounds found in living organisms can only be produced by living organisms and could not be produced in the laboratory.

Friedrich Wohler

Synthesized urea.

Eduard Buchner

Demonstrated the first alcoholic fermentation in a cell-free yeast extract.

Water

The major component of cells that accounts for the high percentage of oxygen.

Nucleus

The control center of the cell that contains the DNA.

Nucleolus

The site for RNA and Ribosome synthesis.

Ribosomes

The site of protein synthesis.

Endoplasmic Reticulum

Part of the cell that detoxifies various drugs.

Golgi Apparatus

Part of the cell that modifies and sorts proteins (transported by vesicles from the ER).

Mitochondria

The major site of ATP production.

Lysosomes

Membraned-enclosed sacs containing hydrolytic enzymes that break down target molecules from outside sources.

Peroxisomes

Contains an enzyme, catalase, that is involved in the metabolism of H2O2.

Cytosol

Portion of the cell that lies outside the nucleus and other membrane-enclosed organelles.

Cytoskeleton

A protein scaffold required for support, internal organization and even movement of the cell.

Spontaneous Process

A reaction that takes place without outside intervention.

Entropy

A measure of disorder or randomness of a system.

Gibbs Free Energy

A useful criterion for predicting the spontaneity of a process.

Gibbs Free Energy is negative (G<0)

Process is spontaneous.

Gibbs Free Energy is positive (G>0)

Process is non-spontaneous.

Gibbs Free Energy is zero (G=0)

Process is at equilibrium with no net-change.

Covalent bond

It is a bond where atoms share electrons. It is formed between atoms that have similar electronegativities.

Specific Heat

It is the amount of heat required to change the temperature of a gram of water 1°C.

Hydrophilic

What are polar molecules called when they interact with water?

Hydrophobic

What are non-polar molecules called when they interact with water?

pH

It is called the "power of Hydrogen"; a measure of the acidity or basicity of the solution.

Amino Acids

The building blocks of proteins.

Codons

Nucleotide triplets that encodes your 20 amino acids.

Chirality center

This will form when an alpha carbon/tetrahedral carbon atom has four different groups bonded to it.

Zwitterion

It is called when an amino acid has both a positive and negative regions.

Essential Amino Acids

This amino acid cannot be synthesized by the body. It must come from food. Also known as Indispensable Amino Acids.

Non-essential Amino Acids

This amino acid can be synthesized by the human body. Also known as Dispensable Amino Acids.

Polar Amino Acids

A type of amino acid which clusters on the surface of soluble proteins and they are hydrophilic.

Non-polar Amino Acids

A type of amino acid which clusters on the surface of membrane proteins and are hydrophobic.

Hydrophobic interaction

A kind of interaction wherein the non-polar side groups are attracted to each other through London dispersion forces. Excludes water and other side chains.

Hydrophilic reaction

A kind of reaction wherein the higher the number of polar groups the more the proteins are soluble. These groups bonds with water and to each other. Excludes non-polar groups.

Ionic interaction

A kind of interaction wherein the presence of acidic or basic side chains leads specific charge where the opposite charges attract. This bond is very strong.

Isoelectric point

It is called when a majority of amino acids molecules in solution have no net charge.

Buffer

It is created when a weak acid is mixed with a salt of the weak acid; or a weak base is mixed with a salt of the weak base. Because of this, solutions resist changes in pH.

Bicarbonate Buffer System

This buffer system manages the acid-base balance produced by both normal and abnormal physiology; also assist in the handling of CO2.

Fibrous proteins

These type of proteins are found only in animals and serves as structural entities—connective tissue, tendons and muscle fiber. Water-insoluble.

Globular Proteins

These type of proteins act as transporters—hemoglobin and enzymes. Water-soluble.

Structure

An important protein function: Skin and bone contain collagen, a fibrous protein.

Catalysis

An important protein function: Enzymes allow reactions to occur in the organism under mild conditions and with great specificity.

Movement

An important protein function: Proteins make up a large protein of muscle fiber and help in the action of various parts of our bodies.

Transport

An important protein function: Moves small molecules through out the organism.

Hormones

An important protein function: Help regulate cell growth.

Protection

An important protein function: Antibodies help rid the body of foreign proteins.

Storage

An important protein function: Help reserve other substances in the organism.

Regulation

An important protein function: Help mediate cell responses.

Heating

Secondary, tertiary and quaternary structures of proteins can be destroyed by: "...breaking of hydrogen bonds."

Changing the pH

Secondary, tertiary and quaternary structures of proteins can be destroyed by: "...protonating or deprotonating the molecule and interrupting ionic interactions."

Reducing agents

Secondary, tertiary and quaternary structures of proteins can be destroyed by: "...breaking disulfide linkages."

Amino Acids

This is the primary structure of a protein.

Peptide bonds

This type of bond will help amino acids join together to form a primary structure.

Dehydration

By this process your peptide bonds are formed.

Tripeptide

This results when a dipeptide is added with a third amino acid.

Secondary Structure

This structure is formed when the protein begins to twist in accordance with chemical forces within the primary chain.

Hydrogen bonds

This type of bond stabilizes the secondary structure.

alpha-helix

It is a spherical structure, consisting of a tightly packed, coiled polypeptide backbone core, with the side chains of the component amino acids extending outward from the central axis.

Proline

An amino acid that creates bends or "kinks" in the primary structure, which inhibit the formation of a regular pattern of hydrogen bonds.

Isoleucine

An amino acid that disrupts the secondary structure.

Glycine

An amino acid that allows too much freedom of movement, which leads to destabilization of the helix.

beta-pleated sheets