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BIOL 1411: Chapter 3
what are the 4 molecules that characterize living things |
protein
carbohydrates
lipids
nucleic acids |
polymers |
large molecules made up of monomers which are covalently bonded |
monomers |
what make up polymers |
what are proteins made up of |
20 amino acids |
what is nucleic acid formed from |
nucleotides |
macromolecules |
polymers with molecular weights exceeding 1,000 |
functional groups |
small groups of atoms |
isomers |
molecules with same chemical formula, same kind & number of atoms but different arrangements |
structural isomers |
differ on how atoms are joined together |
cis-trans isomers |
double bond between 2 carbon atoms |
optical isomers |
carbon atom had 4 different atoms or groups of atoms attached to it
2 different ways of making attachment, mirror-optical |
condensation reactions |
dehydration reactions; loss of water, how polymers formed from monomers |
hydrolysis reaction |
opposite reaction, breakdown of polymers into monomers |
enzymes |
catalyze (speed up) biochemical reactions |
structural proteins |
provide physical stability and movement |
defence proteins |
recognize and respond to nonself substances (antibodies) |
signaling proteins |
control physiology process (hormones) |
receptor proteins |
receive and respond to chemical reactions |
membrane transporters |
regulate passage of substances across cellular membranes |
storage proteins |
store amino acids for later use |
transport proteins |
bind & carry substances within the organism |
proteins |
polymers made of 20 amino acids in different orders |
polypeptide chains |
unbranched (linear) polymers of covalently linked amino acids |
amino acid |
corboxyl functional group & amino functional group attached to same carbon atom |
what makes up an amino acid |
amino group
α carbon
hydrogen atom
carboxyl group
side chain (R group) |
disulfide bridge |
determines how polypeptide chain folds (S-S) |
peptide linkage (peptide bond) |
bond between amino acids in a protein; formed between carboxyl group and amino group |
primary structure of protein |
the sequence of amino acids in a polypeptide chain |
secondary structure of protein |
repeated spacial patterns in different regions of polypeptide chain
α (alpha) helix
β (beta) pleated sheet |
α (alpha) helix |
right-handed coil |
β (beta) pleated sheet |
formed from 2 or more polypeptide chains |
tertiary structure |
when polypeptide chain is bent at specific sites and then folded back and forth |
denatured |
loss of activity of an enzyme or nucleic acid molecule |
quaternary structure |
the ways the polypeptides bind together and interact |
chaperones |
class of proteins that protect 3D shape |