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