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Test your basic knowledge |
MCAT Organic Chemistry 2
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Subjects
:
mcat
,
science
Instructions:
Answer 50 questions in 15 minutes.
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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. Glyceraldehyde
C3H6O3 - with one chiral center
1. presence of strong acids 2. proteolytic enzymes
packing and energy content
D- glyceraldehyde
2. Characteristic of basic amino acids
amphoteric
have amino group in their side chains
lipases
histidine - arginine - lysine
3. Generated btw either thiols on different proteins or thiols on the same protein
disulfide bond
have amino group in their side chains
7.4
unsaturated fatty acid
4. Polar amino acids
absolute configuration
Cause of Amino acid separation in gel electrophoresis
serine - threonine - asparagine - glutamine - cysteine - tyrosine
cysteine and methionine
5. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
anomeric carbon
antiparallel beta sheet
peptide bonds and disulfide bonds
D- amino acid
6. Fxn of cholesterol in the membrane?
only achiral amino acid
modulates fluidity and seeks to maintain optimal fluidity
secondary structure
2 things about the cyclic form of a sugar as an acetal
7. Characteristics of acidic amino acids
histidine - arginine - lysine
have acidic carboxylic acid on side chains - w/ pKa around 4
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
modulates fluidity and seeks to maintain optimal fluidity
8. What kind of lipids compromise the lipid bilayer?
primary structure
phospholipids
peptide bond
van der Waal forces of hydrophobic tails
9. Interconversion btw two anomers
C3H6O3 - with one chiral center
1. presence of strong acids 2. proteolytic enzymes
mutarotation
packing and energy content
10. Name for 6 membered ring
pyranose
isoelectric point
furanose
tertiary structure
11. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
2 things about the cyclic form of a sugar as an acetal
L- configuration
disulfide bond
pI
12. 3 carbon triol that forms backbone of triacylglycerol
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glycogen
only achiral amino acid
glycerol
13. Amino group placed on the right of a fischer projection is a?
D- glyceraldehyde
disulfide bond
D- amino acid
peptide bond
14. D and L describe what?
the basic precursor of the molecule (L or D glyceraldehyde)
ketose
secondary structure
all acidic - basic - and polar amino acids
15. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
isomers
Proteins
L- configuration
van der Waal forces of hydrophobic tails
16. Fatty acid structure
Beta pleated sheet
van der Waal forces of hydrophobic tails
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
Ka
17. 3 physiological roles of lipids
D- glyceraldehyde
isoelectric point
all acidic - basic - and polar amino acids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
18. Enzymes that hydrolyze fats
alpha helix
lipases
disulfide bond
all acidic - basic - and polar amino acids
19. PH at which positive and negative charges balance to form a zwitterion
only amino acid that his a secondary amine
lactase
furanose
pI
20. What configuration do all naturally occuring amino acids have?
L- configuration
1. presence of strong acids 2. proteolytic enzymes
C3H6O3 - with one chiral center
quaternary structure
21. 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
glucose - alpha -1 -2- fructose
ketose
alpha helix
have an R group that is polar enough to H bond - but does no acts an acid or a base
22. Nonpolar - hydrophobic amino acids
peptide bonds and disulfide bonds
pI
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
antiparallel beta sheet
23. Glycosidic linkage of sucrose
triacylglycerol
histidine - arginine - lysine
glucose - alpha -1 -2- fructose
NH2CONH2
24. Fatty acid w/ one or more double bonds in cis form predominately
2 things about the cyclic form of a sugar as an acetal
packing and energy content
anomeric carbon
unsaturated fatty acid
25. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
furanose
optical activity
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
26. Acetic acid formula?
Proteins
CH3COOH
alpha helix
packing and energy content
27. PH at which the amino acid has a net neutral charge
NH2CONH2
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
isoelectric point
has thiol group that allows it the form disulfide bond
28. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
CH3COOH
amphipathic
stereoisomers
epimers
29. Unique feature of cysteine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
has thiol group that allows it the form disulfide bond
glucose - beta -1 -4- glucose
Ka
30. 2 reasons why fats have more efficient energy stores than carbs
tertiary structure
packing and energy content
epimers
7.4
31. Fatty acid w/ no double bonds and maximum number of hydrogens
has thiol group that allows it the form disulfide bond
saturated fatty acid
glucose - alpha -1 -4- glucose
C3H6O3 - with one chiral center
32. Sulfur containing amino acids
Cause of Amino acid separation in gel electrophoresis
D- glyceraldehyde
Proteins
cysteine and methionine
33. Energy storage molecule of carbohydrates for plants
starch
phospholipids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
packing and energy content
34. Sugar with an aldehyde at the first carbon position
D- glyceraldehyde
aldose
modulates fluidity and seeks to maintain optimal fluidity
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
35. 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
mutarotation
the basic precursor of the molecule (L or D glyceraldehyde)
peptide bond
optical activity
36. Hydrophilic amino acids
optical activity
1. presence of strong acids 2. proteolytic enzymes
lactase
all acidic - basic - and polar amino acids
37. Basic amino acids
Beta pleated sheet
histidine - arginine - lysine
disulfide bond
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
38. The amino acid sequence of a protein that is determined by peptide bond
peptide bonds and disulfide bonds
primary structure
7.4
aldose
39. Formula for urea
unsaturated fatty acid
packing and energy content
NH2CONH2
lactase
40. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
the basic precursor of the molecule (L or D glyceraldehyde)
has thiol group that allows it the form disulfide bond
pI
Beta pleated sheet
41. Diastereomers that vary in the configuration of 1 chiral center
cysteine and methionine
epimers
addition of water across of a bond
tertiary structure
42. Characteristics of polar amino acids
only achiral amino acid
all acidic - basic - and polar amino acids
lactase
have an R group that is polar enough to H bond - but does no acts an acid or a base
43. 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
starch
optical activity
glycogen
44. Amino group placed on the left of a fischer projection is a?
L- amino acid
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
ketose
quaternary structure
45. 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
stereoisomers
anomeric carbon
ketose
46. 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
7.4
will have pI of 6
cysteine and methionine
47. Unique feature of proline
peptide bond
peptide bonds and disulfide bonds
isomers
only amino acid that his a secondary amine
48. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
serine - threonine - asparagine - glutamine - cysteine - tyrosine
has thiol group that allows it the form disulfide bond
stereoisomers
49. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
cysteine and methionine
D- amino acid
epimers
50. Name for 5 membered ring
ketose
7.4
pyranose
furanose
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