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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 kind of lipids compromise the lipid bilayer?
triacylglycerol
phospholipids
secondary structure
D- amino acid
2. Sulfur containing amino acids
will have pI of 6
cysteine and methionine
lipases
NH2CONH2
3. Glycosidic linkage of lactose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
lactase
galactose - beta -1 -4- glucose
Beta pleated sheet
4. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
quaternary structure
addition of water across of a bond
has thiol group that allows it the form disulfide bond
5. PH at which the amino acid has a net neutral charge
cysteine and methionine
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
glutamic acid and aspartic acid
isoelectric point
6. Characteristics of hydrophobic amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
lipases
all acidic - basic - and polar amino acids
only amino acid that his a secondary amine
7. Histidine
furanose
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
have an R group that is polar enough to H bond - but does no acts an acid or a base
8. Glycosidic linkage of cellulose
NH2CONH2
7.4
glucose - beta -1 -4- glucose
has thiol group that allows it the form disulfide bond
9. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
serine - threonine - asparagine - glutamine - cysteine - tyrosine
anomeric carbon
have acidic carboxylic acid on side chains - w/ pKa around 4
3 things about the cyclic form of a sugar as a hemiacetal
10. 2 reasons why fats have more efficient energy stores than carbs
van der Waal forces of hydrophobic tails
packing and energy content
C3H6O3 - with one chiral center
antiparallel beta sheet
11. Enzyme that hydrolyzes maltose into 2 glucose molecules?
packing and energy content
maltase
furanose
C3H6O3 - with one chiral center
12. Name for 6 membered ring
pyranose
starch
D- glyceraldehyde
only achiral amino acid
13. Unique feature of proline
only amino acid that his a secondary amine
all acidic - basic - and polar amino acids
D- amino acid
unsaturated fatty acid
14. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glucose - alpha -1 -2- fructose
packing and energy content
addition of water across of a bond
15. 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
anomeric carbon
peptide bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
anomers
16. Diastereomers that vary in the configuration of 1 chiral center
alpha helix
optical activity
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
epimers
17. Unique feature of glycine
furanose
addition of water across of a bond
only achiral amino acid
L- amino acid
18. Fatty acid structure
saturated fatty acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
Characteristics of the peptide bond
D- amino acid
19. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
triacylglycerol
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
phospholipids
20. Hydrophilic amino acids
peptide bond
has thiol group that allows it the form disulfide bond
all acidic - basic - and polar amino acids
epimers
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
amphoteric
D- glyceraldehyde
alpha helix
glutamic acid and aspartic acid
22. Amino group placed on the right of a fischer projection is a?
furanose
D- amino acid
2 things about the cyclic form of a sugar as an acetal
the basic precursor of the molecule (L or D glyceraldehyde)
23. Sugar with an aldehyde at the first carbon position
aldose
Beta pleated sheet
D- glyceraldehyde
C3H6O3 - with one chiral center
24. Physiological pH
alpha helix
has thiol group that allows it the form disulfide bond
7.4
Beta pleated sheet
25. Acetic acid formula?
primary structure
epimers
CH3COOH
packing and energy content
26. 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
only amino acid that his a secondary amine
all acidic - basic - and polar amino acids
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
27. Hydrolysis
C3H6O3 - with one chiral center
ketose
pyranose
addition of water across of a bond
28. Epimers of sugars that vary in the configuration of their anomeric carbons
glucose - beta -1 -4- glucose
anomers
have an R group that is polar enough to H bond - but does no acts an acid or a base
1. presence of strong acids 2. proteolytic enzymes
29. 3 carbon triol that forms backbone of triacylglycerol
lipases
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glycerol
histidine - arginine - lysine
30. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
secondary structure
will have pI of 6
3 things about the cyclic form of a sugar as a hemiacetal
pI
31. Nonpolar - hydrophobic amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
glycogen
L- amino acid
histidine - arginine - lysine
32. 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)
antiparallel beta sheet
van der Waal forces of hydrophobic tails
quaternary structure
primary structure
33. Sugar with a carbonyl group at the 2 carbon position
have an R group that is polar enough to H bond - but does no acts an acid or a base
ketose
cysteine and methionine
CH3COOH
34. Formula for urea
NH2CONH2
D- amino acid
will have pI of 6
amphipathic
35. Molecules with the same atoms - but different bonds
isomers
Beta pleated sheet
histidine - arginine - lysine
peptide bonds and disulfide bonds
36. Molecule can act as a base and as an acid
alpha helix
will have pI of 6
quaternary structure
amphoteric
37. Glycosidic linkage of maltose
lipases
unsaturated fatty acid
glucose - alpha -1 -4- glucose
epimers
38. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
peptide bond
CH3COOH
optical activity
39. Basic amino acids
unsaturated fatty acid
2 things about the cyclic form of a sugar as an acetal
histidine - arginine - lysine
peptide bonds and disulfide bonds
40. Unique feature of cysteine
has thiol group that allows it the form disulfide bond
tertiary structure
aldose
will have pI of 6
41. Enzymes that hydrolyze fats
1. presence of strong acids 2. proteolytic enzymes
all acidic - basic - and polar amino acids
epimers
lipases
42. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
glucose - alpha -1 -2- fructose
1. presence of strong acids 2. proteolytic enzymes
stereoisomers
all acidic - basic - and polar amino acids
43. Characteristic of basic amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
disulfide bond
have amino group in their side chains
epimers
44. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
Cause of Amino acid separation in gel electrophoresis
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
tertiary structure
45. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
Beta pleated sheet
Proteins
glucose - beta -1 -4- glucose
3 things about the cyclic form of a sugar as a hemiacetal
46. The amino acid sequence of a protein that is determined by peptide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
primary structure
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
47. Naturally occurring carbohydrates are formed from what?
all acidic - basic - and polar amino acids
phospholipids
D- amino acid
D- glyceraldehyde
48. What describes the affinity of functional groups for a proton?
furanose
have amino group in their side chains
will have pI of 6
Ka
49. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
anomers
quaternary structure
pI
50. Name for 5 membered ring
stereoisomers
maltase
furanose
pI