ch 3 the macromolecules of the cell Flashcards
(79 cards)
macromolecules
large molecules composed of thousands of covalently connected atoms
4 families of macromolecules
proteins (amino acids)
nucleic acids (nucleotides)
polysaccharides (sugars)
lipids (fatty acids)
polymers are synthesized by
condensation reactions in which activated monomers are linked together by the removal of water
9 major classes of proteins
- enzymes
- structural proteins
- motility proteins
- regulatory proteins
- transport proteins
- signaling proteins
- receptor proteins
- defensive proteins
- storage proteins
enzymes
serve as catalysts, increase the rates of chemical reactions
structural proteins
physical support and shape
ex. keratin and collagen
motility proteins
contraction and movement of cells and intracellular materials
regulatory proteins
control and coordinate cell function
ex. transcription factors such as activators and repressors - ensure that cellular activities are regulated to meet cellular needs
transport proteins
move substances into and out of cells
signaling proteins
communication btw cells
receptor proteins
enable cells to respond to chemical stimuli from the environment
defensive proteins
protect against disease
storage proteins
reservoirs of amino acids and metal ions to be used in later stages of organism development
amino acid components
carboxyl group
amino group
hydrogen atom
r group
alpha carbon
4 broad categories of amino acids
non polar
polar
acidic (- charge)
basic (+ charge)
peptide bond
a covalent bond btw the amino group of one amino acid and the carboxyl group of a second amino acid
- dehydration reaction
N-terminus
the end with the amino group
C-terminus
the end with the carboxyl group
a polypeptide does not become a protein until it has assumed
a unique, stable, three-dimensional shape (conformation), and is biologically active
4 representations of protiens
ribbon model
space-filling model
wire
backbone
monomeric protein
protein that consists of a single polypeptide chain
multimeric protein
protein that consists of two or more polypeptide chains
bonds and interactions important for protein folding and stability
- disulfide bonds (covalent)
- hydrogen bonds
- ionic bonds
- van der waals forces
- hydrophobic interactions
disulfide bonds
covalent bond formed btw two sulfur atoms by oxidation (removal of two hydrogen ions) of sulfhydryl groups
- important in stabilizing the tertiary structure