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