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