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