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