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Test your basic knowledge |
MCAT Organic Chemistry 2
Start Test
Study First
Subjects
:
mcat
,
science
Instructions:
Answer 50 questions in 15 minutes.
If you are not ready to take this test, you can
study here
.
Match each statement with the correct term.
Don't refresh. All questions and answers are randomly picked and ordered every time you load a test.
This is a study tool. The 3 wrong answers for each question are randomly chosen from answers to other questions. So, you might find at times the answers obvious, but you will see it re-enforces your understanding as you take the test each time.
1. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
cysteine and methionine
Beta pleated sheet
Cause of Amino acid separation in gel electrophoresis
glucose - beta -1 -4- glucose
2. Hydrophilic amino acids
histidine - arginine - lysine
has thiol group that allows it the form disulfide bond
all acidic - basic - and polar amino acids
NH2CONH2
3. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
Beta pleated sheet
secondary structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
triacylglycerol
4. Characteristics of polar amino acids
mutarotation
have an R group that is polar enough to H bond - but does no acts an acid or a base
glutamic acid and aspartic acid
L- amino acid
5. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
parallel beta sheet
D- glyceraldehyde
2 things about the cyclic form of a sugar as an acetal
have acidic carboxylic acid on side chains - w/ pKa around 4
6. What kind of lipids compromise the lipid bilayer?
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
phospholipids
glycogen
anomeric carbon
7. Fxn of cholesterol in the membrane?
modulates fluidity and seeks to maintain optimal fluidity
lipases
isoelectric point
serine - threonine - asparagine - glutamine - cysteine - tyrosine
8. Sugar with an aldehyde at the first carbon position
aldose
pI
peptide bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
9. Molecule can act as a base and as an acid
pyranose
amphoteric
furanose
van der Waal forces of hydrophobic tails
10. Glycosidic linkage of lactose
glucose - beta -1 -4- glucose
unsaturated fatty acid
C3H6O3 - with one chiral center
galactose - beta -1 -4- glucose
11. Polar amino acids
triacylglycerol
serine - threonine - asparagine - glutamine - cysteine - tyrosine
modulates fluidity and seeks to maintain optimal fluidity
all acidic - basic - and polar amino acids
12. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
amphoteric
L- amino acid
lipases
13. Enzymes that hydrolyze fats
anomers
lipases
all acidic - basic - and polar amino acids
tertiary structure
14. Sugar with a carbonyl group at the 2 carbon position
anomeric carbon
disulfide bond
3 things about the cyclic form of a sugar as a hemiacetal
ketose
15. Acetic acid formula?
glutamic acid and aspartic acid
CH3COOH
serine - threonine - asparagine - glutamine - cysteine - tyrosine
all acidic - basic - and polar amino acids
16. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
only amino acid that his a secondary amine
unsaturated fatty acid
alpha helix
17. Generated btw either thiols on different proteins or thiols on the same protein
peptide bond
disulfide bond
phospholipids
1. presence of strong acids 2. proteolytic enzymes
18. Interconversion btw two anomers
triacylglycerol
has thiol group that allows it the form disulfide bond
mutarotation
glucose - beta -1 -4- glucose
19. Formula for urea
mutarotation
peptide bond
triacylglycerol
NH2CONH2
20. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
Characteristics of the peptide bond
optical activity
van der Waal forces of hydrophobic tails
unsaturated fatty acid
21. Fatty acid structure
modulates fluidity and seeks to maintain optimal fluidity
glutamic acid and aspartic acid
L- amino acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
22. Unique feature of proline
will have pI of 6
only amino acid that his a secondary amine
quaternary structure
anomers
23. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
NH2CONH2
7.4
Proteins
peptide bond
24. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
amphoteric
parallel beta sheet
absolute configuration
25. Name for 5 membered ring
2 things about the cyclic form of a sugar as an acetal
L- configuration
have amino group in their side chains
furanose
26. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
disulfide bond
furanose
1. presence of strong acids 2. proteolytic enzymes
isomers
27. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
NH2CONH2
primary structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
will have pI of 6
28. Amino group placed on the left of a fischer projection is a?
Cause of Amino acid separation in gel electrophoresis
anomers
L- amino acid
pyranose
29. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
pyranose
optical activity
have amino group in their side chains
30. Naturally occurring carbohydrates are formed from what?
D- glyceraldehyde
anomeric carbon
L- configuration
CH3COOH
31. 1. it exists in solution in equilibrium with linear form 2. mutarotation occurs readily 3. it is a reducing sugar - and reacts positively w/ Benedict's reagent
glucose - beta -1 -4- glucose
3 things about the cyclic form of a sugar as a hemiacetal
saturated fatty acid
have amino group in their side chains
32. Physiological pH
Ka
antiparallel beta sheet
absolute configuration
7.4
33. D and L describe what?
ketose
anomeric carbon
the basic precursor of the molecule (L or D glyceraldehyde)
pI
34. What configuration do all naturally occuring amino acids have?
isoelectric point
peptide bonds and disulfide bonds
L- configuration
isomers
35. Hydrolysis
addition of water across of a bond
pI
tertiary structure
peptide bond
36. PH at which positive and negative charges balance to form a zwitterion
glycerol
CH3COOH
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
pI
37. Epimers of sugars that vary in the configuration of their anomeric carbons
furanose
has thiol group that allows it the form disulfide bond
Ka
anomers
38. Characteristics of acidic amino acids
has thiol group that allows it the form disulfide bond
have acidic carboxylic acid on side chains - w/ pKa around 4
antiparallel beta sheet
triacylglycerol
39. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
primary structure
the basic precursor of the molecule (L or D glyceraldehyde)
cysteine and methionine
parallel beta sheet
40. Unique feature of cysteine
stereoisomers
have amino group in their side chains
has thiol group that allows it the form disulfide bond
7.4
41. Energy storage molecule of carbohydrates for plants
galactose - beta -1 -4- glucose
van der Waal forces of hydrophobic tails
starch
optical activity
42. Acidic amino acids
glutamic acid and aspartic acid
glucose - beta -1 -4- glucose
anomeric carbon
all acidic - basic - and polar amino acids
43. PH at which the amino acid has a net neutral charge
modulates fluidity and seeks to maintain optimal fluidity
anomers
D- amino acid
isoelectric point
44. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
furanose
Proteins
3 things about the cyclic form of a sugar as a hemiacetal
45. What describes the affinity of functional groups for a proton?
D- glyceraldehyde
Ka
mutarotation
pyranose
46. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
glucose - alpha -1 -2- fructose
secondary structure
modulates fluidity and seeks to maintain optimal fluidity
furanose
47. Glycosidic linkage of cellulose
addition of water across of a bond
cysteine and methionine
glucose - beta -1 -4- glucose
absolute configuration
48. Characteristics of hydrophobic amino acids
histidine - arginine - lysine
quaternary structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
only amino acid that his a secondary amine
49. Glyceraldehyde
C3H6O3 - with one chiral center
have an R group that is polar enough to H bond - but does no acts an acid or a base
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
parallel beta sheet
50. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Ka
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
Proteins