SUBJECTS
|
BROWSE
|
CAREER CENTER
|
POPULAR
|
JOIN
|
LOGIN
Business Skills
|
Soft Skills
|
Basic Literacy
|
Certifications
About
|
Help
|
Privacy
|
Terms
|
Email
Search
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. PH at which positive and negative charges balance to form a zwitterion
NH2CONH2
only achiral amino acid
pI
lipases
2. 3 carbon triol that forms backbone of triacylglycerol
amphoteric
glycerol
1. presence of strong acids 2. proteolytic enzymes
alpha helix
3. Formula for urea
NH2CONH2
triacylglycerol
only achiral amino acid
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
4. Fatty acid w/ no double bonds and maximum number of hydrogens
starch
lipases
saturated fatty acid
has thiol group that allows it the form disulfide bond
5. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
alpha helix
Cause of Amino acid separation in gel electrophoresis
has thiol group that allows it the form disulfide bond
the basic precursor of the molecule (L or D glyceraldehyde)
6. Sulfur containing amino acids
cysteine and methionine
lactase
starch
NH2CONH2
7. Unique feature of glycine
only achiral amino acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
stereoisomers
maltase
8. Acetic acid formula?
L- configuration
Proteins
maltase
CH3COOH
9. Glycosidic linkage of sucrose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
Characteristics of the peptide bond
Cause of Amino acid separation in gel electrophoresis
glucose - alpha -1 -2- fructose
10. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
parallel beta sheet
anomers
mutarotation
tertiary structure
11. What describes the affinity of functional groups for a proton?
Ka
have amino group in their side chains
have an R group that is polar enough to H bond - but does no acts an acid or a base
secondary structure
12. Physiological pH
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
glucose - alpha -1 -4- glucose
anomers
7.4
13. Sugar with a carbonyl group at the 2 carbon position
7.4
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
glucose - alpha -1 -2- fructose
ketose
14. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
starch
the basic precursor of the molecule (L or D glyceraldehyde)
have an R group that is polar enough to H bond - but does no acts an acid or a base
15. (R) and (S) describe what?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
absolute configuration
7.4
2 things about the cyclic form of a sugar as an acetal
16. Hydrophilic amino acids
modulates fluidity and seeks to maintain optimal fluidity
unsaturated fatty acid
all acidic - basic - and polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
17. 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
isoelectric point
packing and energy content
alpha helix
anomers
18. Enzyme that hydrolyzes lactose into galactose and glucose into
glucose - beta -1 -4- glucose
lactase
isomers
mutarotation
19. Glyceraldehyde
C3H6O3 - with one chiral center
have acidic carboxylic acid on side chains - w/ pKa around 4
the basic precursor of the molecule (L or D glyceraldehyde)
disulfide bond
20. Hydrolysis
epimers
anomeric carbon
peptide bond
addition of water across of a bond
21. D and L describe what?
the basic precursor of the molecule (L or D glyceraldehyde)
have acidic carboxylic acid on side chains - w/ pKa around 4
only achiral amino acid
7.4
22. Basic amino acids
triacylglycerol
anomers
histidine - arginine - lysine
glycogen
23. Interconversion btw two anomers
C3H6O3 - with one chiral center
isomers
mutarotation
alpha helix
24. Sugar with an aldehyde at the first carbon position
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
starch
aldose
25. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
lipases
saturated fatty acid
26. Energy storage molecule of carbohydrates for animals
saturated fatty acid
primary structure
will have pI of 6
glycogen
27. 2 reasons why fats have more efficient energy stores than carbs
packing and energy content
van der Waal forces of hydrophobic tails
tertiary structure
galactose - beta -1 -4- glucose
28. Characteristics of hydrophobic amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
furanose
lactase
glucose - alpha -1 -2- fructose
29. Molecules with the same atoms - but different bonds
the basic precursor of the molecule (L or D glyceraldehyde)
isomers
only achiral amino acid
D- glyceraldehyde
30. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
packing and energy content
stereoisomers
Characteristics of the peptide bond
has thiol group that allows it the form disulfide bond
31. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
van der Waal forces of hydrophobic tails
ketose
lactase
antiparallel beta sheet
32. Histidine
tertiary structure
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
isomers
anomers
33. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
D- glyceraldehyde
secondary structure
maltase
galactose - beta -1 -4- glucose
34. 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 amino group in their side chains
quaternary structure
all acidic - basic - and polar amino acids
absolute configuration
35. Glycosidic linkage of maltose
packing and energy content
glucose - alpha -1 -2- fructose
glucose - alpha -1 -4- glucose
amphoteric
36. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
7.4
D- glyceraldehyde
cysteine and methionine
Beta pleated sheet
37. 4 causes of denaturation of proteins
C3H6O3 - with one chiral center
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
modulates fluidity and seeks to maintain optimal fluidity
starch
38. Enzymes that hydrolyze fats
triacylglycerol
glucose - beta -1 -4- glucose
packing and energy content
lipases
39. Nonpolar - hydrophobic amino acids
the basic precursor of the molecule (L or D glyceraldehyde)
Proteins
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
40. What configuration do all naturally occuring amino acids have?
epimers
L- configuration
ketose
glucose - alpha -1 -2- fructose
41. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
phospholipids
2 things about the cyclic form of a sugar as an acetal
secondary structure
glucose - alpha -1 -2- fructose
42. Epimers of sugars that vary in the configuration of their anomeric carbons
2 things about the cyclic form of a sugar as an acetal
packing and energy content
lactase
anomers
43. Amino group placed on the left of a fischer projection is a?
L- amino acid
cysteine and methionine
phospholipids
antiparallel beta sheet
44. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
amphipathic
mutarotation
peptide bonds and disulfide bonds
45. What stabilizes lipid bilayer?
lipases
disulfide bond
van der Waal forces of hydrophobic tails
addition of water across of a bond
46. Glycosidic linkage of cellulose
1. presence of strong acids 2. proteolytic enzymes
peptide bonds and disulfide bonds
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glucose - beta -1 -4- glucose
47. (+) and (-) describe what?
pI
C3H6O3 - with one chiral center
optical activity
Ka
48. Molecule can act as a base and as an acid
7.4
will have pI of 6
glucose - beta -1 -4- glucose
amphoteric
49. 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 amino acid that his a secondary amine
have amino group in their side chains
ketose
50. Enzyme that hydrolyzes maltose into 2 glucose molecules?
maltase
phospholipids
Characteristics of the peptide bond
C3H6O3 - with one chiral center