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