Biomolecules Flashcards
Solvency of amino acids with polar R-groups
hydrophilic
Solvency of amino acids with non-polar R-groups
hydrophobic
Number of different R groups in the universe
20 (20 different amino acids)
Oligopeptides
Fewer than 15 amino acids
Peptide
Another name for amino acid. Peptides are short chains of amino acids.
Polypeptide
Greater than 15 amino acids
Peptide Bond
A bond that joins amino acids together. Created through dehydration synthesis.
Primary Protein Structure
A straight chain of amino acids
Secondary Protein Structure
Alpha helix (coiled) or beta-pleated sheet (folded) shapes created when a chain of amino acids is stabilized/held together by hydrogen bonds.
Tertiary Protein Structure
Proteins final, 3-D shape involving ionic, covalent and hydrogen bonds. Interaction of large segments to each other and surrounding water. Vital for function.
Quaternary Protein Structure
2 or more separate polypeptide chains interacting (several tertiary structures working together)
7 Protein Functions
Structure, communication, membrane transport, catalysis, recognition and protection, movement, cell adhesion
3 Key Protein Functions
Structure - shape, muscle, hair, skin
Metabolic - forms enzymes for catalysis
Hormonal - some hormones are proteins (insulin)
Protein Conformation
The overall 3-D shape of protein; vital for function. Protein able to change shape - opening and closing of cell membrane pores.
Protein Denaturation
Drastic conformation change that destroys a protein’s function. Caused by extreme heat or pH. Is often permanent.
3 Factors Affecting Protein Action
High Temperature - denature
pH - denature
Heavy Metals - alter enzyme action
Carbohydrate Fomula
(CH2O)n n = number of carbon atoms
Glucose Formula
glucose has 6 carbon, so formula is C6H12O6
Solvency of Carbs
hydrophilic
Simple Sugar
monosaccharides