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