1what are the monomers of proteins
amino acids
2what does monomers mean
building blocks
3the properties of amino acids are determined by their ___ group
R
4how many molecules of water are required to completely hydroluze a polupeptide made up of 23 amino acids?
22
5what is the function of a collagen
provides strength and support for tissues and organs
6what is an effect of protein denaturation
the three dimensional structure of the protein is altered
7which types of interactions are found in a part of a protein with tertiary but not secondary structure?
disulfide bridges and ionic bonds
8which interaction are found in a part of a protein with secondary structure?
hydrogen bonds
9a channel protein is used to transport ions across a membrane. what would you expect to find lining inside of the channel?
polar amino acids
10which structure is being describe: the interaction of polypeptide subunits and prosthetic groups
quaternary
11which structure is being describe: interactions forming hydrogen bonds between the amino acids
secondary
12which structure is being describe: the sequence of amino acids in the polypeptide chain
primary
13which structure is being describe: the structure formed from interactions between the amino acid side groups
tertiary
14outline the primary protein structure
polypeptide (sequence of amino acids)
15outline the quaternary protein structures
3d structure formed from multiple polypeptide chains
16why are polypeptides called polypeptides?
amino acids are held together with peptide bonds
17what factors can caus denaturation
high temperatures + changes in pH
18Living organisms control pH within their tissues. What is the reason to regulate pH?
Many reactions can only happen at specific pH levels
19what are the functions of proteins and examples of proteins that perform those functions (m-threads)
movement, transport, hormones, receptors, enzymes, defense, structure
20Which variable has effects of enzyme activity?
temperature, pH, subtrate concentration
21how does increasing temp help an exyme find its subtrate
increases kinetic energy of molecules, which makes substrate + enzyme more likely to bump into each other
22distinguish between compeittive and non competitive inhibition
inhibitors are molecules that reduce enzymatic activity. competitive occurs @ active site, non competitive bonds @ allestenic site
23To activate a reaction, what do they have to do witht he energy
lower it
24in enzyme experiments the rate of enzyme activity often gradually decreases. what is most likely to cause this decrease?
the subtrate concentration decreasing
25how do enzymes catalyze chemical reactions?
lower activation energy, so reactions can happen more quickly + efficiently
26describe end product inhibition
the final product of a metaolic pathway inhibits the enzyme in the first step of the pathway
27is it possible to attack a beta galactosidase to alginate beads for use in teh production of lactose free mile. What are teh enzyme that have been attached in this way called?
immobilized
28What is decreased when lactose is added to milk
disaccharides; lactase enzyme breaks down a lactose, a dissacharide
29Why is the enzyme lactase usefuL?
production of lactose free milk so that more people can consume dairy products
30what element is found in an amino acid that was not seen in carbohydrates or lipids
nitrogen
31why do you think amino acids are called amino acids?
-Amino- group + Caboxylic -Acid- Group
32When two things get created, what is that called? how you know?
condensation because anabolic reaction created a bond by remonving a water molecule
33dna holds info for the production of proteins inside the cell. segements of dna are called
genes
34each codon code in a circl is
one amono acid
35polor amino acids are
hydrophiillic
36non polar amino acids are
hydryo phobic
37changed amino acids (+ or -)
hydrophillic
38a protein's secondary structure occurs because of ____ and occurs as the ____
hydrogen bonding; the back bone twists and folds
39what can determine the tertiary structure will be as intermolecular forces and bondsoccur between teh differween r groups based on their polarity and charge
r groups of amino acids
40example movement + function
actin and myosin = muscle contraction
41transport example + function
hemoglobin = quaternary protein -moves oxygen in blood-
42hormones example + function
insulin - regulates blood glucose levels
43receptors example + function
rhodopsin - protein in the retinal cells
44enzymes example + function
rubisco- one of the many enzymes in photosynthesis
45defense example + function
immunoglobulins- antibodies
46structure example + function
collagen - bone, skin, cartiage; spider silk = tougher than silk
47what is teh activation energy
teh minimum amount of energy required to bring reactants to the transition point
48how do enzymes help with activitation energy
lowers energy neededeleased
49enzymes slows reactions. true or false
false, speeds up reactions. wthout it, living humans reactions will be too slow to survive
50what are inhibitors
rhemical substances that binds to enzymes and therefore reduce the activity of enzyme
51describe how a comeptitive inhibitor works to limit enzymatic activity
binds to the active site (substrate is blocked)
52how a noncompetitive inhibitor works to limit enzymatic activity
binds to the enzyme somewhere other than the active site. this changes the shape of the enzyme/active site, so it no longer recongnizes the substrate
53what is allosteric site
the site to which the non competitive inhibitor bound
54is end product inihibition comp. or non comp inhibition
non comp. end products will bind to an allosteric site to change the shape of the active site precenting the process from conitning
55how does this falsify vitalism?
undergoing chemical reactions that create organic products outside of living organisms
56what is the function of a peptide bond
holding amino acids together
57what is peptide bond?
when carbon and nitrogen bonds
58is oxygen positive or negative in c=o
negative partially
59is hydrogen pos or neg at n-h
partially neg