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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. Formula for urea
NH2CONH2
lactase
pI
aldose
2. PH at which positive and negative charges balance to form a zwitterion
Characteristics of the peptide bond
isomers
disulfide bond
pI
3. Epimers of sugars that vary in the configuration of their anomeric carbons
starch
triacylglycerol
L- configuration
anomers
4. 4 causes of denaturation of proteins
ketose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
only achiral amino acid
NH2CONH2
5. Enzyme that hydrolyzes maltose into 2 glucose molecules?
maltase
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
disulfide bond
CH3COOH
6. Generated btw either thiols on different proteins or thiols on the same protein
have acidic carboxylic acid on side chains - w/ pKa around 4
peptide bond
L- configuration
disulfide bond
7. D and L describe what?
glucose - beta -1 -4- glucose
Beta pleated sheet
optical activity
the basic precursor of the molecule (L or D glyceraldehyde)
8. Interaction btw polypeptide subunits arranged in polypeptide. can be covalent bonds or intermolecular forces - disulfide bond that does not form btw residues on the same protein affect (blank)
modulates fluidity and seeks to maintain optimal fluidity
quaternary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
9. 3 carbon triol that forms backbone of triacylglycerol
have amino group in their side chains
glycerol
D- glyceraldehyde
parallel beta sheet
10. Characteristic of basic amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
have amino group in their side chains
will have pI of 6
galactose - beta -1 -4- glucose
11. Basic amino acids
glycogen
has thiol group that allows it the form disulfide bond
histidine - arginine - lysine
antiparallel beta sheet
12. Characteristics of polar amino acids
L- configuration
glycerol
D- amino acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
13. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
lipases
isomers
ketose
1. presence of strong acids 2. proteolytic enzymes
14. Hydrolysis
L- amino acid
L- configuration
have acidic carboxylic acid on side chains - w/ pKa around 4
addition of water across of a bond
15. Glycosidic linkage of cellulose
epimers
anomers
packing and energy content
glucose - beta -1 -4- glucose
16. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
1. presence of strong acids 2. proteolytic enzymes
glycerol
Ka
17. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
amphoteric
ketose
isomers
amphipathic
18. Fatty acid w/ one or more double bonds in cis form predominately
unsaturated fatty acid
the basic precursor of the molecule (L or D glyceraldehyde)
peptide bond
pyranose
19. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
galactose - beta -1 -4- glucose
have an R group that is polar enough to H bond - but does no acts an acid or a base
Characteristics of the peptide bond
7.4
20. Unique feature of glycine
only achiral amino acid
isoelectric point
secondary structure
addition of water across of a bond
21. Molecules with the same atoms - but different bonds
isomers
glucose - alpha -1 -2- fructose
1. presence of strong acids 2. proteolytic enzymes
serine - threonine - asparagine - glutamine - cysteine - tyrosine
22. Energy storage molecule of carbohydrates for animals
glutamic acid and aspartic acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glycogen
Beta pleated sheet
23. Unique feature of cysteine
glucose - alpha -1 -4- glucose
secondary structure
has thiol group that allows it the form disulfide bond
pI
24. (R) and (S) describe what?
primary structure
7.4
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
absolute configuration
25. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
stereoisomers
mutarotation
glucose - alpha -1 -2- fructose
parallel beta sheet
26. Nonpolar - hydrophobic amino acids
lipases
aldose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
alpha helix
27. What kind of lipids compromise the lipid bilayer?
phospholipids
3 things about the cyclic form of a sugar as a hemiacetal
antiparallel beta sheet
histidine - arginine - lysine
28. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
disulfide bond
modulates fluidity and seeks to maintain optimal fluidity
tertiary structure
29. What configuration do all naturally occuring amino acids have?
the basic precursor of the molecule (L or D glyceraldehyde)
isomers
epimers
L- configuration
30. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
triacylglycerol
have amino group in their side chains
serine - threonine - asparagine - glutamine - cysteine - tyrosine
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
31. Fxn of cholesterol in the membrane?
all acidic - basic - and polar amino acids
modulates fluidity and seeks to maintain optimal fluidity
absolute configuration
Beta pleated sheet
32. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
glycerol
disulfide bond
optical activity
33. Unique feature of proline
anomeric carbon
alpha helix
primary structure
only amino acid that his a secondary amine
34. Acidic amino acids
isoelectric point
3 things about the cyclic form of a sugar as a hemiacetal
glutamic acid and aspartic acid
7.4
35. Sugar with an aldehyde at the first carbon position
1. presence of strong acids 2. proteolytic enzymes
disulfide bond
aldose
addition of water across of a bond
36. 2 reasons why fats have more efficient energy stores than carbs
L- configuration
furanose
packing and energy content
mutarotation
37. Characteristics of acidic amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
anomers
ketose
have acidic carboxylic acid on side chains - w/ pKa around 4
38. 2 covalent bonds formed in proteins
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
peptide bonds and disulfide bonds
serine - threonine - asparagine - glutamine - cysteine - tyrosine
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
39. Sugar with a carbonyl group at the 2 carbon position
galactose - beta -1 -4- glucose
antiparallel beta sheet
ketose
3 things about the cyclic form of a sugar as a hemiacetal
40. Hydrophilic amino acids
all acidic - basic - and polar amino acids
Characteristics of the peptide bond
galactose - beta -1 -4- glucose
antiparallel beta sheet
41. Glycosidic linkage of lactose
galactose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glycerol
mutarotation
42. Glyceraldehyde
C3H6O3 - with one chiral center
triacylglycerol
only amino acid that his a secondary amine
saturated fatty acid
43. Amino group placed on the left of a fischer projection is a?
the basic precursor of the molecule (L or D glyceraldehyde)
optical activity
alpha helix
L- amino acid
44. Polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
aldose
peptide bonds and disulfide bonds
have amino group in their side chains
45. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
secondary structure
saturated fatty acid
2 things about the cyclic form of a sugar as an acetal
glucose - beta -1 -4- glucose
46. Glycosidic linkage of maltose
van der Waal forces of hydrophobic tails
glucose - alpha -1 -4- glucose
CH3COOH
NH2CONH2
47. PH at which the amino acid has a net neutral charge
isoelectric point
pyranose
glutamic acid and aspartic acid
modulates fluidity and seeks to maintain optimal fluidity
48. Energy storage molecule of carbohydrates for plants
parallel beta sheet
starch
Proteins
L- amino acid
49. Amino group placed on the right of a fischer projection is a?
secondary structure
D- amino acid
addition of water across of a bond
epimers
50. Fatty acid w/ no double bonds and maximum number of hydrogens
van der Waal forces of hydrophobic tails
pI
Proteins
saturated fatty acid