polymers of nucleotides that store, transmt and express hereditary/genetic info. two types: DNA and RNA
nucleic acids
free energy
the amount of energy in a system that is available to do work
DNA sequence that makes specific proteins
gene
homeostasis
maintaining internal condition (such as pH, body temp)
transcription
after DNA replication, DNA sequences (of bases) being copied into RNA
biological catalysts. all are proteins. always end in "-ase". work by inducing strain or changing orientation of substrate or adding a chemical group
enzyme
gene expression
base sequences are copied from DNA to RNA to specify amino acid sequences in protein
RNA
temporary molecule that can be modified, has OH instead of H so it can be more reactive. single stranded. can fold according to base pairs. info from DNA is transmitted through these to specifcy amino acid sequences of protein
proteins
these are macromolecules. polymers made out of amino acids. They govern chemical reactions in cells and form organism’s structure. Functions include enzymes, receptor, transport and genetic regulation
active site
location on the enzyme where the substrates bind to. it has specifc shape and chemical properties so not any molecule can bind there
after DNA replication, DNA sequences (of bases) being copied into RNA
transcription
polypeptides
longer polymers of peptides with a unique sequence of amino acids. another word for protein
quaternary structure
results from subunites (2+ polypeptide chains binding together). not in al proteins
longer polymers of peptides with a unique sequence of amino acids. another word for protein
polypeptides
covalent bond that connects phosphate to 3' carbon (pentose sugar) to link nucleotides. formed from condensation reactions
phosphodiester bond
a molecule that binds noncovalently to the enzyme's active site and blocks the natural substrate. it is reversible
competitive inhibitor
the amount of energy in a system that is available to do work
free energy
enzyme
biological catalysts. all are proteins. always end in "-ase". work by inducing strain or changing orientation of substrate or adding a chemical group
noncompetitive inhibitor
molecule that binds to an enzyme at a site other than the active site. it causes a change in the shape of the enzyme which alters its activity. the substrate may no longer bind to the active site. if it does, it is reduced. this is reversible. this is a type of allosteric regulation
ions or molecules that some enzymes require in order to function. e.g. metal ions, coenzymes or prosthetic groups
cofactors
molecule that binds to an enzyme at a site other than the active site. it causes a change in the shape of the enzyme which alters its activity. the substrate may no longer bind to the active site. if it does, it is reduced. this is reversible. this is a type of allosteric regulation
noncompetitive inhibitor
beta pleated sheets
interactions between a bunch of R groups. 2+ polypeptide bonds extended. flat portion of potein
alpha helix
in secondary structure of potein. right handed coil/ helix
DNA
polymer of nucleotide subunits (A, T, G, C). stores and transmits genetic info. double stranded. strands run in opposite directions and form a ladder that twists into a double helix. lacks OH group so it is more table. made of pentose sugar, base and phosphate. phosphate and sugar are stable
primary structure of a protein
sequence of amino acids
nucleotide sequence (of bases) in RNA specify sequences of amino acids in proteins
translation
isozymes
enzymes which catalyze the same reaction with different chemical composition and physical properties. can catalyze at different pH/temp. this allows organisms to adapt to changes in the environment
enzymes which catalyze the same reaction with different chemical composition and physical properties. can catalyze at different pH/temp. this allows organisms to adapt to changes in the environment
isozymes
feedback inhibition
when an end product has high concentration, it binds to the commitment step (first) enzyme to make it inactive. binds to either the active site or allosteric site (not active site).
when a non-substrate molecule binds/modifies a site other than the active site of an enzyme. this causes the enzyme to change its shape and changes the rate of reaction or prevents substrate from entering active site. it can also activate an inactive enzyme. types include noncompetitive inhibitor and protein kinases
allosteric regulation
