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