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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. What kind of lipids compromise the lipid bilayer?
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
2 things about the cyclic form of a sugar as an acetal
serine - threonine - asparagine - glutamine - cysteine - tyrosine
phospholipids
2. Nonpolar - hydrophobic amino acids
glutamic acid and aspartic acid
Ka
lactase
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
3. Diastereomers that vary in the configuration of 1 chiral center
have an R group that is polar enough to H bond - but does no acts an acid or a base
tertiary structure
epimers
has thiol group that allows it the form disulfide bond
4. Generated btw either thiols on different proteins or thiols on the same protein
disulfide bond
Proteins
histidine - arginine - lysine
CH3COOH
5. Unique feature of proline
D- glyceraldehyde
saturated fatty acid
only amino acid that his a secondary amine
triacylglycerol
6. Enzyme that hydrolyzes maltose into 2 glucose molecules?
maltase
alpha helix
peptide bonds and disulfide bonds
only achiral amino acid
7. Fxn of cholesterol in the membrane?
starch
modulates fluidity and seeks to maintain optimal fluidity
Ka
2 things about the cyclic form of a sugar as an acetal
8. Epimers of sugars that vary in the configuration of their anomeric carbons
aldose
D- glyceraldehyde
maltase
anomers
9. Glyceraldehyde
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
D- glyceraldehyde
C3H6O3 - with one chiral center
10. Amino group placed on the left of a fischer projection is a?
furanose
quaternary structure
all acidic - basic - and polar amino acids
L- amino acid
11. Characteristics of hydrophobic amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
NH2CONH2
peptide bond
lactase
12. Energy storage molecule of carbohydrates for animals
Beta pleated sheet
triacylglycerol
amphoteric
glycogen
13. Enzyme that hydrolyzes lactose into galactose and glucose into
alpha helix
lactase
anomeric carbon
pI
14. Sugar with a carbonyl group at the 2 carbon position
ketose
glutamic acid and aspartic acid
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
epimers
15. Fatty acid structure
phospholipids
cysteine and methionine
triacylglycerol
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
16. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
isomers
triacylglycerol
has thiol group that allows it the form disulfide bond
maltase
17. Polar amino acids
lipases
serine - threonine - asparagine - glutamine - cysteine - tyrosine
antiparallel beta sheet
quaternary structure
18. 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
isoelectric point
Cause of Amino acid separation in gel electrophoresis
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
19. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
secondary structure
Characteristics of the peptide bond
D- glyceraldehyde
parallel beta sheet
20. Glycosidic linkage of sucrose
have amino group in their side chains
glycerol
glucose - alpha -1 -2- fructose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
21. Physiological pH
parallel beta sheet
7.4
addition of water across of a bond
2 things about the cyclic form of a sugar as an acetal
22. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
optical activity
3 things about the cyclic form of a sugar as a hemiacetal
23. Characteristics of polar amino acids
7.4
ketose
amphoteric
have an R group that is polar enough to H bond - but does no acts an acid or a base
24. Unique feature of glycine
serine - threonine - asparagine - glutamine - cysteine - tyrosine
anomeric carbon
only achiral amino acid
pyranose
25. (R) and (S) describe what?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
absolute configuration
NH2CONH2
galactose - beta -1 -4- glucose
26. D and L describe what?
maltase
secondary structure
the basic precursor of the molecule (L or D glyceraldehyde)
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
27. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Ka
Cause of Amino acid separation in gel electrophoresis
have an R group that is polar enough to H bond - but does no acts an acid or a base
28. Sugar with an aldehyde at the first carbon position
aldose
have an R group that is polar enough to H bond - but does no acts an acid or a base
unsaturated fatty acid
only amino acid that his a secondary amine
29. Glycosidic linkage of cellulose
glucose - beta -1 -4- glucose
Cause of Amino acid separation in gel electrophoresis
modulates fluidity and seeks to maintain optimal fluidity
D- glyceraldehyde
30. What describes the affinity of functional groups for a proton?
2 things about the cyclic form of a sugar as an acetal
tertiary structure
triacylglycerol
Ka
31. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
will have pI of 6
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
secondary structure
unsaturated fatty acid
32. PH at which positive and negative charges balance to form a zwitterion
pI
C3H6O3 - with one chiral center
peptide bonds and disulfide bonds
epimers
33. 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
amphipathic
D- amino acid
isomers
34. Fatty acid w/ one or more double bonds in cis form predominately
pI
L- configuration
primary structure
unsaturated fatty acid
35. 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
starch
alpha helix
quaternary structure
serine - threonine - asparagine - glutamine - cysteine - tyrosine
36. 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)
have acidic carboxylic acid on side chains - w/ pKa around 4
starch
2 things about the cyclic form of a sugar as an acetal
quaternary structure
37. Enzymes that hydrolyze fats
optical activity
mutarotation
amphoteric
lipases
38. Name for 6 membered ring
pyranose
isomers
tertiary structure
phospholipids
39. Molecules with the same atoms - but different bonds
glycogen
isomers
1. presence of strong acids 2. proteolytic enzymes
galactose - beta -1 -4- glucose
40. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
NH2CONH2
galactose - beta -1 -4- glucose
histidine - arginine - lysine
41. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
phospholipids
pyranose
amphipathic
isomers
42. Formula for urea
starch
optical activity
NH2CONH2
aldose
43. Basic amino acids
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
histidine - arginine - lysine
have amino group in their side chains
aldose
44. Naturally occurring carbohydrates are formed from what?
2 things about the cyclic form of a sugar as an acetal
peptide bonds and disulfide bonds
D- glyceraldehyde
has thiol group that allows it the form disulfide bond
45. 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
only achiral amino acid
have acidic carboxylic acid on side chains - w/ pKa around 4
isoelectric point
46. Hydrophilic amino acids
all acidic - basic - and polar amino acids
ketose
pI
have amino group in their side chains
47. Acidic amino acids
Characteristics of the peptide bond
glucose - beta -1 -4- glucose
amphoteric
glutamic acid and aspartic acid
48. Unique feature of cysteine
primary structure
unsaturated fatty acid
has thiol group that allows it the form disulfide bond
L- amino acid
49. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
will have pI of 6
D- amino acid
primary structure
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
50. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
cysteine and methionine
antiparallel beta sheet
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
aldose