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