Biochem Flashcards
(43 cards)
Catabolism
Breakdown reactions
Anabolism
Reactions of synthesis
Biopolymers
Form from condensation synthesis reactions which involve the elimination of a water molecule; made of smaller monomer units; includes: proteins, carbohydrates, and enzymes
Condensation
Reactions involving the elimination of a water molecule
Hydrolysis
The process of breaking up a biopolymer back into its monomer units by the addition of water
Amino Acids
The monomer units that make up a proteins (ex: Glycine and Alanine); Always has an amine group and a carboxylic acid group
Zwitter Ion
A form which amino acids can take where when placed in a neutral solution will donate a proton from the carboxyl group (acting as an acid) and also accept a proton through the amine group (acting as a base) and therefore forms an ion with both a positive and negative charge.
Isoelectric Point
pH where the amino acid will exist as a zwitter ion
Anionic Amino Acid
Form an amino acid takes in a strongly alkaline solution having a negative charge.
Cationic Amino Acid
Form an amino acid takes in a strongly acidic solution having a positive charge
Peptide/Amide link
Occurs when the carboxyl group of an amino acid undergoes a condensation reaction with the amine group of another creating a polypeptide with the functional group -CONH-
Protein
Polypeptide made up of more than 50 amino acid monomers
Primary Structure
amino acids forming the linear sequence of the polypeptide chain; hold together by covalent or peptide bonds; sequence of the protein is unique to that protein.
Secondary Structure
Regions of the chain are organized into regular structures known as alpha-helixes and beta pleated sheets; held together by hydrogen bonds between the lone pairs of the O in the carboxyl group and an H of an amine group further down the line
Tertiary Structure
Held together by the interaction of the side change through ionic interactions, hydrogen bonds, dispersion forces, or disulfide links to form the three dimensional shape of a protein
Quaternary Structure
How the individual polypeptide chains interact with each other
Enzyme
Protein that acts as a biological catalyst, increasing reaction rates of biological reactions without being used up in the process; tend to have more than 200 amino acids and are specifically designed for only one type of reaction through its tertiary structure.
Substrate
The specific protein that will “unlock” an enzyme allowing it to catalyze the reaction.
Electrophloresis
Analytical technique to create a “protein fingerprint” by separating large molecules with an overall charge and mass such as DNA and Proteins
Lipids
Molecules including oils and fats (triglycerides), phospholipids, and steroids; mainly carbon and hydrogen with small amounts of oxygen and other elements; nonpolar and so are insoluble in water; store energy in the body, release more energy per gram than carbs; thermal insulator
Free fatty acid
Long hydrocarbon tail with a carboxylic acid group head
Triglyceride
3 fatty acid molecules attached to a glycerol (OH-OH-OH) through a ester link formed by a condensation reaction
Phospholipids
Similar structure to triglyceride but replacing one of the fatty acids with phosphate group; polar head (hydrophilic), 2 non-polar tails (hydrophobic) forming a bilayer; forms cell membranes
Steroids
Lipids with a structure consisting of 4 fused rings known as the steroidal backbone