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