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Secondary Structure = Formation of helices, beta-pleated sheet, strands (turns and loops). Involves
primary structure. Structure was formed based on Hydrogen bonding (H and O)
Tertiary Structure = Involvement of both primary and R-group. Combination of Polar, Non Polar,
Uncharge, Charge, (combination of 2nd structure)
Aliphatic = Linear
Aromatic = Ring
R-group/side chains = determine the different structure and chemical properties of an amino acid
Amino Group (H2N) + Carboxyl Group (COOH) + R Group (side chain) = AMINO ACID
Denaturation = destruction of both the quaternary and tertiary structures to primary or secondary
structure. High structure can be broken down to lower structure.
Ways to denaturalized = Heat, Alcohol Disrupts Hydrogen Bonding, Acids and Bases Disrupt Salt Bridges,
Heavy Metal Salts Disrupt Disulfide Bonds, Reducing Agents Disrupt Disulfide Bonds
What is Protein = Protein is a macronutrient that is essential for the formation of structure, function,
and regulation of the body’s tissues and organs.
What are the essential proteins? Proteins that can’t be produced in the body. 9 amino acids
What are the non-essential proteins? Proteins that can be produced but sometimes are essential due to
body stress causing it not to produce such essential proteins. 11 amino acids
What are the different categories of amino acids? Polar (hydrophilic) - Non Polar (hydrophobic) , Acid -
Base - Neutral, Aromatic
You can change a neutral amino acid by changing charges, sulfur, acidic (2 carboxyl, 1 base), base (1
carboxyl, 1 base)
N-terminal is the head (contains amino group) C-terminal is the tail (contains the carboxyl group)
Zwitterion = parts are charged but it is neutral (one negative, one positive)