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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. Enzyme that hydrolyzes lactose into galactose and glucose into
Beta pleated sheet
isomers
glutamic acid and aspartic acid
lactase
2. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
anomers
glutamic acid and aspartic acid
Cause of Amino acid separation in gel electrophoresis
C3H6O3 - with one chiral center
3. Glycosidic linkage of cellulose
glucose - beta -1 -4- glucose
isomers
L- amino acid
packing and energy content
4. 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
7.4
isoelectric point
5. Hydrophilic amino acids
galactose - beta -1 -4- glucose
antiparallel beta sheet
all acidic - basic - and polar amino acids
peptide bond
6. Energy storage molecule of carbohydrates for plants
quaternary structure
starch
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
CH3COOH
7. Sugar with a carbonyl group at the 2 carbon position
unsaturated fatty acid
alpha helix
ketose
3 things about the cyclic form of a sugar as a hemiacetal
8. What describes the affinity of functional groups for a proton?
isomers
galactose - beta -1 -4- glucose
Ka
C3H6O3 - with one chiral center
9. 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
NH2CONH2
maltase
serine - threonine - asparagine - glutamine - cysteine - tyrosine
alpha helix
10. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
Ka
Beta pleated sheet
L- configuration
secondary structure
11. 2 covalent bonds formed in proteins
quaternary structure
peptide bonds and disulfide bonds
L- configuration
isomers
12. Fatty acid w/ one or more double bonds in cis form predominately
optical activity
antiparallel beta sheet
unsaturated fatty acid
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
13. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
modulates fluidity and seeks to maintain optimal fluidity
Beta pleated sheet
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
quaternary structure
14. Sugar with an aldehyde at the first carbon position
primary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
tertiary structure
aldose
15. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
Characteristics of the peptide bond
glycerol
only achiral amino acid
16. Polar amino acids
stereoisomers
ketose
1. presence of strong acids 2. proteolytic enzymes
serine - threonine - asparagine - glutamine - cysteine - tyrosine
17. Characteristics of hydrophobic amino acids
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
7.4
furanose
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
18. Characteristic of basic amino acids
Beta pleated sheet
have amino group in their side chains
histidine - arginine - lysine
absolute configuration
19. Unique feature of cysteine
primary structure
have acidic carboxylic acid on side chains - w/ pKa around 4
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
has thiol group that allows it the form disulfide bond
20. Diastereomers that vary in the configuration of 1 chiral center
epimers
glycogen
the basic precursor of the molecule (L or D glyceraldehyde)
only achiral amino acid
21. What configuration do all naturally occuring amino acids have?
L- configuration
lipases
glucose - beta -1 -4- glucose
glycerol
22. Epimers of sugars that vary in the configuration of their anomeric carbons
anomers
glycerol
D- glyceraldehyde
lactase
23. Characteristics of polar amino acids
have an R group that is polar enough to H bond - but does no acts an acid or a base
absolute configuration
glucose - alpha -1 -4- glucose
stereoisomers
24. PH at which positive and negative charges balance to form a zwitterion
maltase
pI
Ka
antiparallel beta sheet
25. Molecules with the same atoms - but different bonds
epimers
isomers
isoelectric point
have amino group in their side chains
26. Fatty acid w/ no double bonds and maximum number of hydrogens
glucose - alpha -1 -2- fructose
only amino acid that his a secondary amine
saturated fatty acid
anomers
27. Unique feature of glycine
epimers
modulates fluidity and seeks to maintain optimal fluidity
only achiral amino acid
quaternary structure
28. D and L describe what?
NH2CONH2
only achiral amino acid
tertiary structure
the basic precursor of the molecule (L or D glyceraldehyde)
29. Hydrolysis
3 things about the cyclic form of a sugar as a hemiacetal
triacylglycerol
addition of water across of a bond
lactase
30. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
alpha helix
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
have acidic carboxylic acid on side chains - w/ pKa around 4
31. Name for 5 membered ring
primary structure
van der Waal forces of hydrophobic tails
furanose
L- amino acid
32. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
amphipathic
Beta pleated sheet
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
33. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
amphoteric
antiparallel beta sheet
lipases
ketose
34. Enzyme that hydrolyzes maltose into 2 glucose molecules?
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
C3H6O3 - with one chiral center
maltase
anomeric carbon
35. Fatty acid structure
addition of water across of a bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
lactase
histidine - arginine - lysine
36. 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
isomers
Proteins
peptide bond
serine - threonine - asparagine - glutamine - cysteine - tyrosine
37. Glycosidic linkage of maltose
stereoisomers
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
peptide bond
glucose - alpha -1 -4- glucose
38. 2 reasons why fats have more efficient energy stores than carbs
saturated fatty acid
glucose - beta -1 -4- glucose
packing and energy content
pyranose
39. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
7.4
glucose - alpha -1 -2- fructose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
40. Amino group placed on the left of a fischer projection is a?
L- amino acid
only amino acid that his a secondary amine
packing and energy content
Cause of Amino acid separation in gel electrophoresis
41. 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
addition of water across of a bond
3 things about the cyclic form of a sugar as a hemiacetal
quaternary structure
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
42. Unique feature of proline
L- configuration
only amino acid that his a secondary amine
glutamic acid and aspartic acid
L- amino acid
43. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
primary structure
parallel beta sheet
all acidic - basic - and polar amino acids
histidine - arginine - lysine
44. Glycosidic linkage of sucrose
amphipathic
peptide bonds and disulfide bonds
glucose - alpha -1 -2- fructose
D- amino acid
45. Characteristics of acidic amino acids
secondary structure
glucose - alpha -1 -4- glucose
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
have acidic carboxylic acid on side chains - w/ pKa around 4
46. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
has thiol group that allows it the form disulfide bond
triacylglycerol
galactose - beta -1 -4- glucose
47. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
Ka
anomers
triacylglycerol
stereoisomers
48. Nonpolar - hydrophobic amino acids
will have pI of 6
NH2CONH2
L- amino acid
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
49. Name for 6 membered ring
pyranose
amphoteric
glycogen
glutamic acid and aspartic acid
50. Energy storage molecule of carbohydrates for animals
quaternary structure
aldose
galactose - beta -1 -4- glucose
glycogen