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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. PH at which the amino acid has a net neutral charge
Proteins
isoelectric point
alpha helix
isomers
2. Diastereomers that vary in the configuration of 1 chiral center
glucose - alpha -1 -4- glucose
primary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
epimers
3. Fatty acid w/ no double bonds and maximum number of hydrogens
lactase
optical activity
saturated fatty acid
antiparallel beta sheet
4. Naturally occurring carbohydrates are formed from what?
isomers
Proteins
addition of water across of a bond
D- glyceraldehyde
5. Unique feature of glycine
have an R group that is polar enough to H bond - but does no acts an acid or a base
have amino group in their side chains
lipases
only achiral amino acid
6. Name for 5 membered ring
lactase
glucose - alpha -1 -4- glucose
furanose
unsaturated fatty acid
7. Characteristics of polar amino acids
glucose - beta -1 -4- glucose
7.4
have an R group that is polar enough to H bond - but does no acts an acid or a base
lactase
8. 2 reasons why fats have more efficient energy stores than carbs
aldose
van der Waal forces of hydrophobic tails
packing and energy content
only amino acid that his a secondary amine
9. Fxn of cholesterol in the membrane?
modulates fluidity and seeks to maintain optimal fluidity
anomeric carbon
Characteristics of the peptide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
10. 3 carbon triol that forms backbone of triacylglycerol
epimers
glycerol
Beta pleated sheet
disulfide bond
11. Epimers of sugars that vary in the configuration of their anomeric carbons
anomers
pI
has thiol group that allows it the form disulfide bond
only achiral amino acid
12. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
the basic precursor of the molecule (L or D glyceraldehyde)
amphipathic
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Proteins
13. Sulfur containing amino acids
cysteine and methionine
histidine - arginine - lysine
peptide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
14. Acetic acid formula?
CH3COOH
glucose - beta -1 -4- glucose
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
histidine - arginine - lysine
15. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
cysteine and methionine
have amino group in their side chains
amphipathic
1. presence of strong acids 2. proteolytic enzymes
16. (+) and (-) describe what?
pI
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
optical activity
triacylglycerol
17. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
triacylglycerol
phospholipids
stereoisomers
2 things about the cyclic form of a sugar as an acetal
18. Energy storage molecule of carbohydrates for plants
peptide bond
D- amino acid
starch
addition of water across of a bond
19. What stabilizes lipid bilayer?
pI
van der Waal forces of hydrophobic tails
only achiral amino acid
C3H6O3 - with one chiral center
20. Amino group placed on the right of a fischer projection is a?
glycogen
D- amino acid
phospholipids
primary structure
21. Sugar with a carbonyl group at the 2 carbon position
glycerol
ketose
starch
phospholipids
22. Enzyme that hydrolyzes maltose into 2 glucose molecules?
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
quaternary structure
maltase
disulfide bond
23. What configuration do all naturally occuring amino acids have?
D- amino acid
only achiral amino acid
L- configuration
mutarotation
24. 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
isoelectric point
quaternary structure
modulates fluidity and seeks to maintain optimal fluidity
25. 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
all acidic - basic - and polar amino acids
furanose
van der Waal forces of hydrophobic tails
peptide bond
26. Fatty acid structure
aldose
only amino acid that his a secondary amine
ketose
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
27. Characteristics of hydrophobic amino acids
amphoteric
have amino group in their side chains
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
starch
28. Molecule can act as a base and as an acid
will have pI of 6
glycogen
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
amphoteric
29. D and L describe what?
only amino acid that his a secondary amine
primary structure
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
the basic precursor of the molecule (L or D glyceraldehyde)
30. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
optical activity
lipases
primary structure
31. 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
amphipathic
have an R group that is polar enough to H bond - but does no acts an acid or a base
all acidic - basic - and polar amino acids
alpha helix
32. The amino acid sequence of a protein that is determined by peptide bond
primary structure
the basic precursor of the molecule (L or D glyceraldehyde)
will have pI of 6
anomeric carbon
33. Formula for urea
packing and energy content
glucose - alpha -1 -4- glucose
NH2CONH2
furanose
34. What describes the affinity of functional groups for a proton?
Characteristics of the peptide bond
anomeric carbon
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Ka
35. Polar amino acids
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
serine - threonine - asparagine - glutamine - cysteine - tyrosine
stereoisomers
packing and energy content
36. 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
addition of water across of a bond
absolute configuration
3 things about the cyclic form of a sugar as a hemiacetal
unsaturated fatty acid
37. Basic amino acids
C3H6O3 - with one chiral center
Beta pleated sheet
histidine - arginine - lysine
glycerol
38. Fatty acid w/ one or more double bonds in cis form predominately
unsaturated fatty acid
anomeric carbon
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
isoelectric point
39. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
epimers
Characteristics of the peptide bond
has thiol group that allows it the form disulfide bond
optical activity
40. Enzyme that hydrolyzes lactose into galactose and glucose into
glutamic acid and aspartic acid
isoelectric point
lactase
glucose - beta -1 -4- glucose
41. Glycosidic linkage of cellulose
glucose - beta -1 -4- glucose
aldose
glucose - alpha -1 -4- glucose
D- amino acid
42. Physiological pH
epimers
7.4
packing and energy content
absolute configuration
43. Hydrophilic amino acids
anomeric carbon
all acidic - basic - and polar amino acids
glycogen
peptide bond
44. 4 causes of denaturation of proteins
only achiral amino acid
glycogen
van der Waal forces of hydrophobic tails
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
45. Glycosidic linkage of lactose
amphipathic
aldose
ketose
galactose - beta -1 -4- glucose
46. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
pI
triacylglycerol
galactose - beta -1 -4- glucose
pyranose
47. 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
2 things about the cyclic form of a sugar as an acetal
peptide bonds and disulfide bonds
glycogen
48. 2 covalent bonds formed in proteins
D- glyceraldehyde
peptide bonds and disulfide bonds
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
absolute configuration
49. Unique feature of proline
glycerol
isoelectric point
van der Waal forces of hydrophobic tails
only amino acid that his a secondary amine
50. Characteristic of basic amino acids
D- glyceraldehyde
have amino group in their side chains
peptide bond
alpha helix