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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. Enzyme that hydrolyzes maltose into 2 glucose molecules?
glycogen
maltase
glycerol
antiparallel beta sheet
2. Characteristics of acidic amino acids
1. presence of strong acids 2. proteolytic enzymes
ketose
have acidic carboxylic acid on side chains - w/ pKa around 4
have amino group in their side chains
3. Hydrophilic amino acids
all acidic - basic - and polar amino acids
glutamic acid and aspartic acid
anomers
lipases
4. 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)
L- amino acid
pyranose
L- configuration
quaternary structure
5. Epimers of sugars that vary in the configuration of their anomeric carbons
anomers
mutarotation
peptide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
6. Amino group placed on the right of a fischer projection is a?
D- amino acid
isoelectric point
van der Waal forces of hydrophobic tails
isomers
7. Fatty acid w/ one or more double bonds in cis form predominately
7.4
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
unsaturated fatty acid
8. 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
glucose - alpha -1 -2- fructose
peptide bond
lipases
9. Energy storage molecule of carbohydrates for animals
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
have amino group in their side chains
glycogen
stereoisomers
10. 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
3 things about the cyclic form of a sugar as a hemiacetal
have an R group that is polar enough to H bond - but does no acts an acid or a base
disulfide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
11. Acetic acid formula?
CH3COOH
lactase
7.4
antiparallel beta sheet
12. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
saturated fatty acid
2 things about the cyclic form of a sugar as an acetal
only amino acid that his a secondary amine
D- glyceraldehyde
13. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
optical activity
ketose
Cause of Amino acid separation in gel electrophoresis
lipases
14. Interconversion btw two anomers
glycerol
amphoteric
have amino group in their side chains
mutarotation
15. Sulfur containing amino acids
cysteine and methionine
L- configuration
pyranose
CH3COOH
16. 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
quaternary structure
glycogen
alpha helix
cysteine and methionine
17. Fatty acid w/ no double bonds and maximum number of hydrogens
saturated fatty acid
only achiral amino acid
glycogen
primary structure
18. Glyceraldehyde
tertiary structure
maltase
C3H6O3 - with one chiral center
aldose
19. What kind of lipids compromise the lipid bilayer?
amphoteric
L- configuration
phospholipids
NH2CONH2
20. Characteristic of basic amino acids
have amino group in their side chains
galactose - beta -1 -4- glucose
Cause of Amino acid separation in gel electrophoresis
D- glyceraldehyde
21. Hydrolysis
addition of water across of a bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
will have pI of 6
peptide bonds and disulfide bonds
22. Basic amino acids
glucose - alpha -1 -4- glucose
histidine - arginine - lysine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
23. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
glutamic acid and aspartic acid
stereoisomers
glycerol
parallel beta sheet
24. Name for 5 membered ring
peptide bond
furanose
Proteins
histidine - arginine - lysine
25. Unique feature of proline
2 things about the cyclic form of a sugar as an acetal
only amino acid that his a secondary amine
glycogen
amphipathic
26. (R) and (S) describe what?
L- configuration
starch
1. presence of strong acids 2. proteolytic enzymes
absolute configuration
27. 4 causes of denaturation of proteins
aldose
Ka
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
will have pI of 6
28. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
cysteine and methionine
secondary structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
1. presence of strong acids 2. proteolytic enzymes
29. Glycosidic linkage of cellulose
galactose - beta -1 -4- glucose
addition of water across of a bond
glycerol
glucose - beta -1 -4- glucose
30. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
anomers
triacylglycerol
isoelectric point
Ka
31. What describes the affinity of functional groups for a proton?
secondary structure
D- amino acid
Ka
1. presence of strong acids 2. proteolytic enzymes
32. D and L describe what?
the basic precursor of the molecule (L or D glyceraldehyde)
only amino acid that his a secondary amine
glycogen
glutamic acid and aspartic acid
33. Sugar with a carbonyl group at the 2 carbon position
modulates fluidity and seeks to maintain optimal fluidity
stereoisomers
alpha helix
ketose
34. (+) and (-) describe what?
NH2CONH2
disulfide bond
have amino group in their side chains
optical activity
35. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
will have pI of 6
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
addition of water across of a bond
36. Nonpolar - hydrophobic amino acids
packing and energy content
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
addition of water across of a bond
37. Histidine
secondary structure
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
ketose
38. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
absolute configuration
3 things about the cyclic form of a sugar as a hemiacetal
stereoisomers
39. 2 covalent bonds formed in proteins
will have pI of 6
peptide bonds and disulfide bonds
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
Characteristics of the peptide bond
40. Polar amino acids
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
pyranose
2 things about the cyclic form of a sugar as an acetal
serine - threonine - asparagine - glutamine - cysteine - tyrosine
41. 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
unsaturated fatty acid
Beta pleated sheet
L- amino acid
42. What stabilizes lipid bilayer?
L- configuration
van der Waal forces of hydrophobic tails
glucose - alpha -1 -4- glucose
Characteristics of the peptide bond
43. Glycosidic linkage of maltose
glucose - alpha -1 -4- glucose
all acidic - basic - and polar amino acids
D- glyceraldehyde
furanose
44. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
pyranose
antiparallel beta sheet
disulfide bond
ketose
45. Unique feature of cysteine
van der Waal forces of hydrophobic tails
has thiol group that allows it the form disulfide bond
glucose - alpha -1 -2- fructose
7.4
46. What configuration do all naturally occuring amino acids have?
has thiol group that allows it the form disulfide bond
ketose
L- configuration
anomers
47. Physiological pH
maltase
7.4
histidine - arginine - lysine
C3H6O3 - with one chiral center
48. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
furanose
tertiary structure
anomeric carbon
have an R group that is polar enough to H bond - but does no acts an acid or a base
49. Diastereomers that vary in the configuration of 1 chiral center
anomeric carbon
epimers
starch
L- configuration
50. Naturally occurring carbohydrates are formed from what?
pyranose
D- glyceraldehyde
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
absolute configuration