Physiology Quiz 1 (covering packets 1-4): Packet 1 review

Helpfulness: 0
Set Details Share
created 7 years ago by Malibudentist
51 views
updated 7 years ago by Malibudentist
Subjects:
physiology
show moreless
Page to share:
Embed this setcancel
COPY
code changes based on your size selection
Size:
X
Show:
1

One theme of physiology is hierarchy. Name the hierarchy starting from atoms

atoms, molecules, cells, tissues, organs, organ systems

2

example of inorganic(2 examples)and organic (4examples) materials in the body

inorganic: water, ions
organic: carb, fats, proteins, nucleic acids

3

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.

4

Name all type of intermolecular forces in secondary and tertiary structure (4 examples in tertiary)

secondary: H-bonds
tertiary: covalent (disulfide bridge), non-covalent (H bonds, ionic, van der Waals)

5

in quaternary structure, seaparate chains of amino acids, aka ________ associate covalently/noncovalntly to form _____ protein

subunits, non-covalently, multimeric

6

In protein binding, two things matter, which are

protein shape, distribution of charges

7

a ligand is

ion or molecule that binds to protein

8

pick the right properties of ligand: their bind to protein through electrical/hydrophobic attractions, the binding is weak/strong

both, weak

9

ligand bids at the _______ portion of the protein

binding site

10

3 properties of binding sites

specificity, affinity, saturation

11

all three properties of binding sites are affected by what?

protein's shape and charge distribution

12

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)

13

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

14

when a ligand binds to the functional binding site,

it produces the protein's physiological function.

15

two ways the modulatory molecule bind to the ___________ to bring change:

regulatory binding site, allosteric and covalent bonding

16

two big difference between covalent, allosteric bonding

1) covalent bodning versus non covalent bonding
2) uses ATP dephosphorylation versus uses small molecules

17

catabolism is? anabolism is?

breakdown and synthesis of ORGANIC molecules

18

3 things that affects reaction rate

concentration, temperature, Ea/catalyst (enzyme) usuage

19

both coenzymes and cofactors are ________. but coenzyme is ______ while cofactors are ______. A big exmaple of coenzyme is_____

non-protein molecule, organic, non-organic, vitamins

20

cofactors are involved in _____ process

catalysis

21

IMPORTANT: coenzyme cofactor relationship is that

coenzyme is a type of cofactor.

22

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

23

what is apoenzyme? what is the whole protein called with the cofactors and the coenzymes?

just the protein part, holoenzyme

24

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.

25

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

26

making more products leads to more/less synthesis due to_____

less, negative feedback (phophofructokinase)