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