Physiology Quiz 1 (covering packets 1-4): Packet 1 review
One theme of physiology is hierarchy. Name the hierarchy starting from atoms
atoms, molecules, cells, tissues, organs, organ systems
example of inorganic(2 examples)and organic (4examples) materials in the body
inorganic: water, ions
organic: carb, fats, proteins, nucleic acids
Another big theme is regulation, aka ______. ______ molecule provide such regulation in two ways. describe the two ways
homeostasis. proteins. enzyme work, changing confirmation to turn chemical function off by restricting or opening binding sites.
Name all type of intermolecular forces in secondary and tertiary structure (4 examples in tertiary)
tertiary: covalent (disulfide bridge), non-covalent (H bonds, ionic, van der Waals)
in quaternary structure, seaparate chains of amino acids, aka ________ associate covalently/noncovalntly to form _____ protein
subunits, non-covalently, multimeric
In protein binding, two things matter, which are
protein shape, distribution of charges
a ligand is
ion or molecule that binds to protein
pick the right properties of ligand: their bind to protein through electrical/hydrophobic attractions, the binding is weak/strong
ligand bids at the _______ portion of the protein
3 properties of binding sites
specificity, affinity, saturation
all three properties of binding sites are affected by what?
protein's shape and charge distribution
binding of a ligand is important because two reasons
affect function, affect other binding site in the same protein (both due to change in shape)
A modulatory molecule is a ligand that binds in the _________ as opposed to _____________ what is an example of it?
"regulatory binding site" "functional binding site" to restrict other ligand, O2
when a ligand binds to the functional binding site,
it produces the protein's physiological function.
two ways the modulatory molecule bind to the ___________ to bring change:
regulatory binding site, allosteric and covalent bonding
two big difference between covalent, allosteric bonding
1) covalent bodning versus non covalent bonding
2) uses ATP dephosphorylation versus uses small molecules
catabolism is? anabolism is?
breakdown and synthesis of ORGANIC molecules
3 things that affects reaction rate
concentration, temperature, Ea/catalyst (enzyme) usuage
both coenzymes and cofactors are ________. but coenzyme is ______ while cofactors are ______. A big exmaple of coenzyme is_____
non-protein molecule, organic, non-organic, vitamins
cofactors are involved in _____ process
IMPORTANT: coenzyme cofactor relationship is that
coenzyme is a type of cofactor.
cofactors are distinguished in two large groups: coenzymes and ________. the difference between the two is that coenzymes are ______ while prosthetic groups are ______. therefore coenzymes are often treated like______
prosthetic groups. loose bound, tight bound, enzyme substrate
what is apoenzyme? what is the whole protein called with the cofactors and the coenzymes?
just the protein part, holoenzyme
describe reversible and irreversible reactions in terms of 1) Energy released 2)product,reactant concentration
reversible rxn release little E, product conc is a bit higher. irreversible releases lots of E, product conc is very high because most reactants are converted.
definition of 1)metabolic pathway 2)rate-limit reaction
1) chained reactions catalyzed by enzymes 2) slowest reaction in chain that determines rate of pathway
making more products leads to more/less synthesis due to_____
less, negative feedback (phophofructokinase)