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