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