Unit 1: Chemistry of Life Flashcards
Name the Functional Groups (7)
Methyl - (R-Ch3)
Hydroxyl - (R-OH)
Carbonyl- (R-CO)
Carboxyl - (R-COOH)
Amine - (R-NH2)
Sulfhydryl - (R-SH)
Phosphate - (R-PO4^3-)
Name Macromolecules (4)
definition: Cells join smaller organic molecules together to form larger molecules.
Carbs - Sugar (glucose) - glycosidic bond
Fat/Lipids - Fatty Acid, Glycerol- ester bond
Proteins - Amino Acids- peptide bond
Nucleic Acid - Nucleotide phosphate, 5 carbon sugar, A/G/T/C nitrogen bond
Protein & Function
- instrumental in about everything that an organism does; the overwhelming enzymes in cells and regulate metabolism by selectively accelerating chemical bonds
-Functions: structural support, storage. transport of other substances, intercellular signaling, movement, and defense against foreign substances
-most structurally complex molecules known
- protein polymers are constructed from the set of amino acids (20 monomers)
-polymers of protein are called polypeptides
polypeptide
- a polymer of amino acids connected in a specific sequence
Amino Acid Structure
consists of four components: attracted to central carbon (alpha carbon), hydrogen atom (above), a carboxyl group (right), an amino group (left), a variable “R’’ group -> side chain(below)
Macromolecules
Cells join smaller organic molecules together to form larger molecules.
Folding of a Protein: Primary Structure
- The primary structure of a protein is its unique sequence of amino acids.
-The precise primary structure of a protein is determined by inherited genetic information.
Folding of a Protein: Secondary Structure
- results from hydrogen bonds at regular intervals along the polypeptide backbone
Typical shapes that develop from the secondary structure are coils (an alpha helix) or folds (beta pleated sheets).
Folding of a Protein: Tertiary Structure
- Tertiary structure is determined by various interactions among R groups and between R groups and the polypeptide backbone.
- These interactions include hydrogen bonds among polar and/or charged areas, ionic bonds between charged R groups, and Hydrophobic interactions and van der Waals interactions among hydrophobic R groups
Folding of a Protein: Quaternary Structure
Quarternary structure results from the aggregation of two or more polypeptide subunits.
Collagen is a fibrous protein of three supercoiled polypeptides like a rope.
This provides the structural strength for their role in connective tissue.
Hemoglobin is a globular protein with two copies of two kinds of polypeptides
Glucose drawing (alpha and beta)
(Refer to notes for drawings)
triglyceride drawing
(refer to notes)
Parts of an atom: atomic number, mass number, atomic mass,
Atomic number = # of protons = # of electrons
mass number = # of protons + # of neutrons
Atomic mass = average weight of an element with respect with to its isotopes
Hydrolysis
involves adding water to one large molecule to split-multiple smaller molecules
dehydration reaction
reactions in which molecules combine to become macromolecules by the removal of a H atom and an OH group between them,(covalent bond is form)
