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