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