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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. What stabilizes lipid bilayer?
2 things about the cyclic form of a sugar as an acetal
D- glyceraldehyde
only amino acid that his a secondary amine
van der Waal forces of hydrophobic tails
2. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
van der Waal forces of hydrophobic tails
tertiary structure
L- configuration
3. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
amphipathic
2 things about the cyclic form of a sugar as an acetal
glucose - alpha -1 -4- glucose
will have pI of 6
4. Naturally occurring carbohydrates are formed from what?
serine - threonine - asparagine - glutamine - cysteine - tyrosine
phospholipids
unsaturated fatty acid
D- glyceraldehyde
5. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
starch
glucose - beta -1 -4- glucose
amphipathic
serine - threonine - asparagine - glutamine - cysteine - tyrosine
6. Glycosidic linkage of cellulose
glucose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
tertiary structure
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
7. Unique feature of proline
only amino acid that his a secondary amine
anomers
packing and energy content
pyranose
8. Enzyme that hydrolyzes maltose into 2 glucose molecules?
glycogen
maltase
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
peptide bonds and disulfide bonds
9. Diastereomers that vary in the configuration of 1 chiral center
glucose - beta -1 -4- glucose
Cause of Amino acid separation in gel electrophoresis
epimers
lactase
10. Glycosidic linkage of lactose
pI
galactose - beta -1 -4- glucose
histidine - arginine - lysine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
11. Name for 5 membered ring
has thiol group that allows it the form disulfide bond
serine - threonine - asparagine - glutamine - cysteine - tyrosine
furanose
Characteristics of the peptide bond
12. Acidic amino acids
starch
have amino group in their side chains
saturated fatty acid
glutamic acid and aspartic acid
13. Fxn of cholesterol in the membrane?
D- amino acid
lipases
mutarotation
modulates fluidity and seeks to maintain optimal fluidity
14. Unique feature of glycine
serine - threonine - asparagine - glutamine - cysteine - tyrosine
only achiral amino acid
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
Cause of Amino acid separation in gel electrophoresis
15. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
parallel beta sheet
NH2CONH2
starch
CH3COOH
16. Molecule can act as a base and as an acid
epimers
amphoteric
modulates fluidity and seeks to maintain optimal fluidity
have an R group that is polar enough to H bond - but does no acts an acid or a base
17. 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
alpha helix
pI
lipases
triacylglycerol
18. 2 covalent bonds formed in proteins
amphipathic
2 things about the cyclic form of a sugar as an acetal
quaternary structure
peptide bonds and disulfide bonds
19. PH at which the amino acid has a net neutral charge
NH2CONH2
lipases
isomers
isoelectric point
20. Energy storage molecule of carbohydrates for plants
mutarotation
amphipathic
starch
saturated fatty acid
21. Generated btw either thiols on different proteins or thiols on the same protein
lipases
peptide bond
the basic precursor of the molecule (L or D glyceraldehyde)
disulfide bond
22. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
L- configuration
saturated fatty acid
glucose - alpha -1 -4- glucose
23. What describes the affinity of functional groups for a proton?
3 things about the cyclic form of a sugar as a hemiacetal
Ka
have an R group that is polar enough to H bond - but does no acts an acid or a base
lipases
24. D and L describe what?
only achiral amino acid
peptide bond
the basic precursor of the molecule (L or D glyceraldehyde)
Beta pleated sheet
25. Enzymes that hydrolyze fats
lipases
absolute configuration
D- glyceraldehyde
1. presence of strong acids 2. proteolytic enzymes
26. Characteristics of acidic amino acids
have an R group that is polar enough to H bond - but does no acts an acid or a base
all acidic - basic - and polar amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
optical activity
27. Polar amino acids
Characteristics of the peptide bond
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
serine - threonine - asparagine - glutamine - cysteine - tyrosine
parallel beta sheet
28. 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
disulfide bond
parallel beta sheet
3 things about the cyclic form of a sugar as a hemiacetal
furanose
29. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
amphipathic
Proteins
disulfide bond
C3H6O3 - with one chiral center
30. (R) and (S) describe what?
serine - threonine - asparagine - glutamine - cysteine - tyrosine
CH3COOH
absolute configuration
anomeric carbon
31. Sulfur containing amino acids
cysteine and methionine
histidine - arginine - lysine
D- amino acid
the basic precursor of the molecule (L or D glyceraldehyde)
32. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
anomeric carbon
has thiol group that allows it the form disulfide bond
anomers
Characteristics of the peptide bond
33. PH at which positive and negative charges balance to form a zwitterion
have amino group in their side chains
lactase
Ka
pI
34. Unique feature of cysteine
has thiol group that allows it the form disulfide bond
unsaturated fatty acid
absolute configuration
alpha helix
35. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
glutamic acid and aspartic acid
disulfide bond
stereoisomers
36. 2 reasons why fats have more efficient energy stores than carbs
pI
Proteins
all acidic - basic - and polar amino acids
packing and energy content
37. 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
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
packing and energy content
optical activity
38. Nonpolar - hydrophobic amino acids
glucose - beta -1 -4- glucose
peptide bond
histidine - arginine - lysine
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
39. Covalent bond formed btw carboxyl group of one atom and the amino group of another amino acid in an addition - elimination mechanism - enzymes are required to carry out rxn
optical activity
peptide bond
anomers
galactose - beta -1 -4- glucose
40. Fatty acid structure
the basic precursor of the molecule (L or D glyceraldehyde)
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
has thiol group that allows it the form disulfide bond
C3H6O3 - with one chiral center
41. Sugar with an aldehyde at the first carbon position
aldose
furanose
glycerol
modulates fluidity and seeks to maintain optimal fluidity
42. Interconversion btw two anomers
isomers
only amino acid that his a secondary amine
isoelectric point
mutarotation
43. Hydrophilic amino acids
all acidic - basic - and polar amino acids
3 things about the cyclic form of a sugar as a hemiacetal
peptide bond
peptide bonds and disulfide bonds
44. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
peptide bonds and disulfide bonds
glycerol
tertiary structure
Characteristics of the peptide bond
45. 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
antiparallel beta sheet
2 things about the cyclic form of a sugar as an acetal
quaternary structure
46. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
pyranose
Cause of Amino acid separation in gel electrophoresis
saturated fatty acid
packing and energy content
47. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
only achiral amino acid
have acidic carboxylic acid on side chains - w/ pKa around 4
isoelectric point
48. Amino group placed on the left of a fischer projection is a?
unsaturated fatty acid
L- amino acid
maltase
packing and energy content
49. Name for 6 membered ring
pyranose
optical activity
L- amino acid
alpha helix
50. Epimers of sugars that vary in the configuration of their anomeric carbons
histidine - arginine - lysine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
anomers
tertiary structure