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MCAT Organic Chemistry 2
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Subjects
:
mcat
,
science
Instructions:
Answer 50 questions in 15 minutes.
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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. What describes the affinity of functional groups for a proton?
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
Ka
cysteine and methionine
the basic precursor of the molecule (L or D glyceraldehyde)
2. Acidic amino acids
has thiol group that allows it the form disulfide bond
glutamic acid and aspartic acid
L- configuration
antiparallel beta sheet
3. Sugar with an aldehyde at the first carbon position
aldose
glycerol
galactose - beta -1 -4- glucose
has thiol group that allows it the form disulfide bond
4. What stabilizes lipid bilayer?
ketose
L- amino acid
alpha helix
van der Waal forces of hydrophobic tails
5. Fxn of cholesterol in the membrane?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
addition of water across of a bond
modulates fluidity and seeks to maintain optimal fluidity
have acidic carboxylic acid on side chains - w/ pKa around 4
6. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
triacylglycerol
D- amino acid
tertiary structure
7. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
isoelectric point
glutamic acid and aspartic acid
CH3COOH
8. Enzyme that hydrolyzes lactose into galactose and glucose into
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glycogen
lactase
ketose
9. Nonpolar - hydrophobic amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
van der Waal forces of hydrophobic tails
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glycerol
10. Glycosidic linkage of sucrose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
glucose - alpha -1 -2- fructose
van der Waal forces of hydrophobic tails
the basic precursor of the molecule (L or D glyceraldehyde)
11. Unique feature of cysteine
galactose - beta -1 -4- glucose
has thiol group that allows it the form disulfide bond
furanose
2 things about the cyclic form of a sugar as an acetal
12. Polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
addition of water across of a bond
CH3COOH
histidine - arginine - lysine
13. Hydrolysis
anomers
addition of water across of a bond
tertiary structure
parallel beta sheet
14. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
antiparallel beta sheet
Cause of Amino acid separation in gel electrophoresis
lactase
L- amino acid
15. Unique feature of proline
anomeric carbon
furanose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
only amino acid that his a secondary amine
16. Epimers of sugars that vary in the configuration of their anomeric carbons
amphoteric
anomers
peptide bond
L- configuration
17. Basic amino acids
unsaturated fatty acid
D- amino acid
histidine - arginine - lysine
L- amino acid
18. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
stereoisomers
histidine - arginine - lysine
anomers
serine - threonine - asparagine - glutamine - cysteine - tyrosine
19. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
packing and energy content
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
triacylglycerol
2 things about the cyclic form of a sugar as an acetal
20. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
packing and energy content
quaternary structure
ketose
21. Fatty acid structure
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
stereoisomers
L- configuration
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
22. 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)
NH2CONH2
quaternary structure
serine - threonine - asparagine - glutamine - cysteine - tyrosine
absolute configuration
23. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
epimers
antiparallel beta sheet
amphoteric
pI
24. Amino group placed on the left of a fischer projection is a?
L- amino acid
only amino acid that his a secondary amine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
CH3COOH
25. Amino group placed on the right of a fischer projection is a?
peptide bond
D- amino acid
NH2CONH2
anomeric carbon
26. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
NH2CONH2
amphipathic
Beta pleated sheet
D- glyceraldehyde
27. Glyceraldehyde
3 things about the cyclic form of a sugar as a hemiacetal
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
C3H6O3 - with one chiral center
alpha helix
28. 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
mutarotation
only achiral amino acid
primary structure
29. Generated btw either thiols on different proteins or thiols on the same protein
cysteine and methionine
only achiral amino acid
tertiary structure
disulfide bond
30. Name for 5 membered ring
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
have an R group that is polar enough to H bond - but does no acts an acid or a base
amphoteric
furanose
31. Characteristics of polar amino acids
all acidic - basic - and polar amino acids
starch
glutamic acid and aspartic acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
32. Hydrophilic amino acids
lipases
L- amino acid
all acidic - basic - and polar amino acids
addition of water across of a bond
33. (R) and (S) describe what?
absolute configuration
glucose - beta -1 -4- glucose
unsaturated fatty acid
furanose
34. What kind of lipids compromise the lipid bilayer?
glycerol
disulfide bond
phospholipids
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
35. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
parallel beta sheet
tertiary structure
Proteins
have an R group that is polar enough to H bond - but does no acts an acid or a base
36. Glycosidic linkage of lactose
anomers
3 things about the cyclic form of a sugar as a hemiacetal
galactose - beta -1 -4- glucose
glucose - alpha -1 -2- fructose
37. Sulfur containing amino acids
optical activity
2 things about the cyclic form of a sugar as an acetal
cysteine and methionine
pI
38. (+) and (-) describe what?
glutamic acid and aspartic acid
disulfide bond
glycerol
optical activity
39. PH at which positive and negative charges balance to form a zwitterion
optical activity
L- amino acid
pI
quaternary structure
40. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
will have pI of 6
have acidic carboxylic acid on side chains - w/ pKa around 4
antiparallel beta sheet
van der Waal forces of hydrophobic tails
41. 3 physiological roles of lipids
C3H6O3 - with one chiral center
CH3COOH
triacylglycerol
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
42. Interconversion btw two anomers
alpha helix
mutarotation
glucose - alpha -1 -4- glucose
NH2CONH2
43. Acetic acid formula?
CH3COOH
furanose
amphoteric
glycerol
44. 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
aldose
D- glyceraldehyde
pyranose
45. Molecule can act as a base and as an acid
D- amino acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
amphoteric
ketose
46. Unique feature of glycine
only achiral amino acid
modulates fluidity and seeks to maintain optimal fluidity
glucose - alpha -1 -2- fructose
Characteristics of the peptide bond
47. D and L describe what?
secondary structure
L- configuration
only achiral amino acid
the basic precursor of the molecule (L or D glyceraldehyde)
48. Fatty acid w/ one or more double bonds in cis form predominately
has thiol group that allows it the form disulfide bond
unsaturated fatty acid
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
primary structure
49. What configuration do all naturally occuring amino acids have?
unsaturated fatty acid
Ka
peptide bond
L- configuration
50. Enzyme that hydrolyzes maltose into 2 glucose molecules?
3 things about the cyclic form of a sugar as a hemiacetal
maltase
starch
has thiol group that allows it the form disulfide bond
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