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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. Energy storage molecule of carbohydrates for plants
has thiol group that allows it the form disulfide bond
secondary structure
starch
isomers
2. The amino acid sequence of a protein that is determined by peptide bond
primary structure
isoelectric point
optical activity
anomers
3. Epimers of sugars that vary in the configuration of their anomeric carbons
glucose - beta -1 -4- glucose
anomers
Beta pleated sheet
have an R group that is polar enough to H bond - but does no acts an acid or a base
4. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
quaternary structure
glucose - alpha -1 -4- glucose
mutarotation
anomeric carbon
5. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
glucose - alpha -1 -2- fructose
Proteins
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
tertiary structure
6. 2 reasons why fats have more efficient energy stores than carbs
lactase
L- amino acid
packing and energy content
stereoisomers
7. 3 carbon triol that forms backbone of triacylglycerol
glycerol
packing and energy content
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
peptide bond
8. Physiological pH
secondary structure
7.4
has thiol group that allows it the form disulfide bond
lactase
9. Glycosidic linkage of lactose
peptide bonds and disulfide bonds
galactose - beta -1 -4- glucose
only amino acid that his a secondary amine
isomers
10. Enzyme that hydrolyzes lactose into galactose and glucose into
has thiol group that allows it the form disulfide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
lactase
packing and energy content
11. Fxn of cholesterol in the membrane?
D- amino acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
unsaturated fatty acid
modulates fluidity and seeks to maintain optimal fluidity
12. Unique feature of cysteine
lipases
secondary structure
anomers
has thiol group that allows it the form disulfide bond
13. Energy storage molecule of carbohydrates for animals
glycogen
isoelectric point
7.4
phospholipids
14. Glyceraldehyde
Characteristics of the peptide bond
C3H6O3 - with one chiral center
have amino group in their side chains
lipases
15. PH at which the amino acid has a net neutral charge
aldose
isoelectric point
optical activity
amphoteric
16. Characteristics of acidic amino acids
phospholipids
quaternary structure
pI
have acidic carboxylic acid on side chains - w/ pKa around 4
17. Interconversion btw two anomers
has thiol group that allows it the form disulfide bond
mutarotation
only achiral amino acid
only amino acid that his a secondary amine
18. PH at which positive and negative charges balance to form a zwitterion
pI
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
Cause of Amino acid separation in gel electrophoresis
stereoisomers
19. Naturally occurring carbohydrates are formed from what?
all acidic - basic - and polar amino acids
ketose
D- glyceraldehyde
pI
20. Diastereomers that vary in the configuration of 1 chiral center
stereoisomers
epimers
optical activity
galactose - beta -1 -4- glucose
21. Acetic acid formula?
CH3COOH
anomers
primary structure
quaternary structure
22. Generated btw either thiols on different proteins or thiols on the same protein
serine - threonine - asparagine - glutamine - cysteine - tyrosine
2 things about the cyclic form of a sugar as an acetal
histidine - arginine - lysine
disulfide bond
23. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
tertiary structure
1. presence of strong acids 2. proteolytic enzymes
phospholipids
24. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
van der Waal forces of hydrophobic tails
parallel beta sheet
lactase
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
25. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
will have pI of 6
D- glyceraldehyde
glucose - beta -1 -4- glucose
primary structure
26. 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)
lipases
anomers
disulfide bond
quaternary structure
27. Glycosidic linkage of sucrose
D- glyceraldehyde
pyranose
alpha helix
glucose - alpha -1 -2- fructose
28. Sugar with an aldehyde at the first carbon position
saturated fatty acid
aldose
disulfide bond
L- amino acid
29. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
Proteins
Characteristics of the peptide bond
unsaturated fatty acid
glucose - beta -1 -4- glucose
30. Characteristic of basic amino acids
pyranose
has thiol group that allows it the form disulfide bond
glycogen
have amino group in their side chains
31. 2 covalent bonds formed in proteins
tertiary structure
D- glyceraldehyde
peptide bonds and disulfide bonds
van der Waal forces of hydrophobic tails
32. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
Cause of Amino acid separation in gel electrophoresis
absolute configuration
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
disulfide bond
33. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
glutamic acid and aspartic acid
amphipathic
D- glyceraldehyde
isomers
34. Glycosidic linkage of maltose
packing and energy content
D- amino acid
alpha helix
glucose - alpha -1 -4- glucose
35. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
Characteristics of the peptide bond
peptide bonds and disulfide bonds
36. (+) and (-) describe what?
quaternary structure
peptide bonds and disulfide bonds
optical activity
anomers
37. D and L describe what?
only amino acid that his a secondary amine
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
the basic precursor of the molecule (L or D glyceraldehyde)
38. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
C3H6O3 - with one chiral center
CH3COOH
peptide bonds and disulfide bonds
triacylglycerol
39. Formula for urea
starch
D- glyceraldehyde
NH2CONH2
anomers
40. Hydrophilic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
ketose
all acidic - basic - and polar amino acids
antiparallel beta sheet
41. Name for 6 membered ring
pyranose
amphoteric
furanose
anomers
42. Right handed helix w/ carboxyl of one amino acid bound to the amine of another amino acid three residues away - proline never resides in this structure b/c it would place a kink in the helix
lactase
glutamic acid and aspartic acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
alpha helix
43. Amino group placed on the left of a fischer projection is a?
CH3COOH
anomeric carbon
L- amino acid
only achiral amino acid
44. Characteristics of polar amino acids
have an R group that is polar enough to H bond - but does no acts an acid or a base
quaternary structure
optical activity
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
45. Enzyme that hydrolyzes maltose into 2 glucose molecules?
addition of water across of a bond
maltase
D- glyceraldehyde
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
46. What describes the affinity of functional groups for a proton?
serine - threonine - asparagine - glutamine - cysteine - tyrosine
quaternary structure
histidine - arginine - lysine
Ka
47. Unique feature of proline
ketose
only amino acid that his a secondary amine
galactose - beta -1 -4- glucose
modulates fluidity and seeks to maintain optimal fluidity
48. What stabilizes lipid bilayer?
saturated fatty acid
van der Waal forces of hydrophobic tails
have an R group that is polar enough to H bond - but does no acts an acid or a base
alpha helix
49. Hydrolysis
serine - threonine - asparagine - glutamine - cysteine - tyrosine
addition of water across of a bond
unsaturated fatty acid
anomers
50. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
isoelectric point
1. presence of strong acids 2. proteolytic enzymes
peptide bonds and disulfide bonds