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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?
pI
maltase
NH2CONH2
has thiol group that allows it the form disulfide bond
2. Unique feature of glycine
all acidic - basic - and polar amino acids
ketose
maltase
only achiral amino acid
3. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
alpha helix
amphipathic
L- configuration
packing and energy content
4. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
glycogen
anomeric carbon
furanose
3 things about the cyclic form of a sugar as a hemiacetal
5. 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)
C3H6O3 - with one chiral center
optical activity
quaternary structure
Proteins
6. Amino group placed on the left of a fischer projection is a?
Characteristics of the peptide bond
L- amino acid
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
galactose - beta -1 -4- glucose
7. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
have an R group that is polar enough to H bond - but does no acts an acid or a base
amphipathic
triacylglycerol
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
8. Nonpolar - hydrophobic amino acids
phospholipids
disulfide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
amphoteric
9. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
ketose
Characteristics of the peptide bond
stereoisomers
will have pI of 6
10. D and L describe what?
D- amino acid
secondary structure
glucose - beta -1 -4- glucose
the basic precursor of the molecule (L or D glyceraldehyde)
11. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
glucose - alpha -1 -2- fructose
Beta pleated sheet
1. presence of strong acids 2. proteolytic enzymes
D- glyceraldehyde
12. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
parallel beta sheet
pI
glucose - beta -1 -4- glucose
Proteins
13. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
anomeric carbon
1. presence of strong acids 2. proteolytic enzymes
serine - threonine - asparagine - glutamine - cysteine - tyrosine
D- glyceraldehyde
14. Name for 5 membered ring
isoelectric point
peptide bond
phospholipids
furanose
15. Enzyme that hydrolyzes lactose into galactose and glucose into
alpha helix
anomeric carbon
galactose - beta -1 -4- glucose
lactase
16. Acetic acid formula?
Characteristics of the peptide bond
maltase
CH3COOH
disulfide bond
17. Physiological pH
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
ketose
anomers
7.4
18. 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
glycerol
D- glyceraldehyde
only amino acid that his a secondary amine
19. Unique feature of cysteine
disulfide bond
glucose - alpha -1 -2- fructose
has thiol group that allows it the form disulfide bond
L- configuration
20. Characteristics of hydrophobic amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
1. presence of strong acids 2. proteolytic enzymes
tertiary structure
antiparallel beta sheet
21. Molecules with the same atoms - but different bonds
unsaturated fatty acid
pI
isomers
tertiary structure
22. Energy storage molecule of carbohydrates for animals
have amino group in their side chains
glycogen
Ka
have acidic carboxylic acid on side chains - w/ pKa around 4
23. Epimers of sugars that vary in the configuration of their anomeric carbons
maltase
C3H6O3 - with one chiral center
anomers
anomeric carbon
24. Glycosidic linkage of lactose
disulfide bond
has thiol group that allows it the form disulfide bond
galactose - beta -1 -4- glucose
epimers
25. Hydrolysis
3 things about the cyclic form of a sugar as a hemiacetal
addition of water across of a bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
2 things about the cyclic form of a sugar as an acetal
26. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
triacylglycerol
phospholipids
anomeric carbon
27. Name for 6 membered ring
pyranose
glucose - alpha -1 -4- glucose
D- glyceraldehyde
tertiary structure
28. What configuration do all naturally occuring amino acids have?
2 things about the cyclic form of a sugar as an acetal
L- configuration
glucose - beta -1 -4- glucose
D- glyceraldehyde
29. Acidic amino acids
3 things about the cyclic form of a sugar as a hemiacetal
pI
glutamic acid and aspartic acid
all acidic - basic - and polar amino acids
30. The amino acid sequence of a protein that is determined by peptide bond
have amino group in their side chains
primary structure
amphoteric
peptide bonds and disulfide bonds
31. 3 carbon triol that forms backbone of triacylglycerol
Ka
parallel beta sheet
glycerol
tertiary structure
32. Formula for urea
only achiral amino acid
C3H6O3 - with one chiral center
D- glyceraldehyde
NH2CONH2
33. Fatty acid structure
has thiol group that allows it the form disulfide bond
modulates fluidity and seeks to maintain optimal fluidity
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
optical activity
34. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
lactase
mutarotation
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
antiparallel beta sheet
35. Characteristics of polar amino acids
quaternary structure
isoelectric point
aldose
have an R group that is polar enough to H bond - but does no acts an acid or a base
36. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
alpha helix
van der Waal forces of hydrophobic tails
Characteristics of the peptide bond
mutarotation
37. Interconversion btw two anomers
1. presence of strong acids 2. proteolytic enzymes
C3H6O3 - with one chiral center
glucose - beta -1 -4- glucose
mutarotation
38. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
isoelectric point
Characteristics of the peptide bond
peptide bond
39. 2 covalent bonds formed in proteins
serine - threonine - asparagine - glutamine - cysteine - tyrosine
have an R group that is polar enough to H bond - but does no acts an acid or a base
isoelectric point
peptide bonds and disulfide bonds
40. Sulfur containing amino acids
Cause of Amino acid separation in gel electrophoresis
anomeric carbon
Ka
cysteine and methionine
41. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
disulfide bond
modulates fluidity and seeks to maintain optimal fluidity
Beta pleated sheet
Cause of Amino acid separation in gel electrophoresis
42. Basic amino acids
Cause of Amino acid separation in gel electrophoresis
primary structure
histidine - arginine - lysine
only achiral amino acid
43. Glycosidic linkage of maltose
packing and energy content
galactose - beta -1 -4- glucose
2 things about the cyclic form of a sugar as an acetal
glucose - alpha -1 -4- glucose
44. Unique feature of proline
triacylglycerol
only amino acid that his a secondary amine
has thiol group that allows it the form disulfide bond
tertiary structure
45. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
stereoisomers
2 things about the cyclic form of a sugar as an acetal
antiparallel beta sheet
46. Characteristics of acidic amino acids
cysteine and methionine
anomeric carbon
have acidic carboxylic acid on side chains - w/ pKa around 4
quaternary structure
47. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
secondary structure
amphoteric
NH2CONH2
48. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
mutarotation
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
parallel beta sheet
only amino acid that his a secondary amine
49. Sugar with an aldehyde at the first carbon position
have amino group in their side chains
aldose
antiparallel beta sheet
mutarotation
50. (R) and (S) describe what?
Proteins
serine - threonine - asparagine - glutamine - cysteine - tyrosine
2 things about the cyclic form of a sugar as an acetal
absolute configuration