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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. Amino group placed on the right of a fischer projection is a?
D- amino acid
L- configuration
histidine - arginine - lysine
epimers
2. Fatty acid structure
Characteristics of the peptide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
absolute configuration
C3H6O3 - with one chiral center
3. Fatty acid w/ no double bonds and maximum number of hydrogens
unsaturated fatty acid
saturated fatty acid
only achiral amino acid
serine - threonine - asparagine - glutamine - cysteine - tyrosine
4. Molecule can act as a base and as an acid
galactose - beta -1 -4- glucose
3 things about the cyclic form of a sugar as a hemiacetal
anomeric carbon
amphoteric
5. 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
ketose
primary structure
1. presence of strong acids 2. proteolytic enzymes
alpha helix
6. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
unsaturated fatty acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
Proteins
peptide bonds and disulfide bonds
7. Fatty acid w/ one or more double bonds in cis form predominately
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
unsaturated fatty acid
histidine - arginine - lysine
8. Diastereomers that vary in the configuration of 1 chiral center
glycogen
epimers
3 things about the cyclic form of a sugar as a hemiacetal
van der Waal forces of hydrophobic tails
9. Sugar with an aldehyde at the first carbon position
maltase
aldose
isoelectric point
D- glyceraldehyde
10. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
furanose
C3H6O3 - with one chiral center
has thiol group that allows it the form disulfide bond
will have pI of 6
11. 2 covalent bonds formed in proteins
addition of water across of a bond
maltase
NH2CONH2
peptide bonds and disulfide bonds
12. Enzyme that hydrolyzes lactose into galactose and glucose into
3 things about the cyclic form of a sugar as a hemiacetal
galactose - beta -1 -4- glucose
lactase
addition of water across of a bond
13. Sulfur containing amino acids
all acidic - basic - and polar amino acids
amphipathic
cysteine and methionine
only achiral amino acid
14. Polar amino acids
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
epimers
serine - threonine - asparagine - glutamine - cysteine - tyrosine
disulfide bond
15. Name for 5 membered ring
peptide bonds and disulfide bonds
furanose
Characteristics of the peptide bond
phospholipids
16. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
Cause of Amino acid separation in gel electrophoresis
alpha helix
CH3COOH
Characteristics of the peptide bond
17. Glycosidic linkage of cellulose
7.4
cysteine and methionine
glucose - beta -1 -4- glucose
van der Waal forces of hydrophobic tails
18. PH at which the amino acid has a net neutral charge
CH3COOH
ketose
isoelectric point
maltase
19. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
packing and energy content
parallel beta sheet
Cause of Amino acid separation in gel electrophoresis
peptide bonds and disulfide bonds
20. Enzymes that hydrolyze fats
furanose
phospholipids
lipases
7.4
21. 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)
quaternary structure
amphoteric
only achiral amino acid
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
22. (+) and (-) describe what?
optical activity
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
isomers
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
23. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
amphipathic
stereoisomers
mutarotation
phospholipids
24. Hydrophilic amino acids
aldose
packing and energy content
all acidic - basic - and polar amino acids
lactase
25. 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
starch
lipases
1. presence of strong acids 2. proteolytic enzymes
3 things about the cyclic form of a sugar as a hemiacetal
26. 3 carbon triol that forms backbone of triacylglycerol
all acidic - basic - and polar amino acids
glycerol
peptide bonds and disulfide bonds
starch
27. Characteristics of acidic amino acids
only achiral amino acid
van der Waal forces of hydrophobic tails
glycogen
have acidic carboxylic acid on side chains - w/ pKa around 4
28. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
unsaturated fatty acid
disulfide bond
29. Generated btw either thiols on different proteins or thiols on the same protein
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
pyranose
have an R group that is polar enough to H bond - but does no acts an acid or a base
disulfide bond
30. PH at which positive and negative charges balance to form a zwitterion
serine - threonine - asparagine - glutamine - cysteine - tyrosine
primary structure
peptide bonds and disulfide bonds
pI
31. What describes the affinity of functional groups for a proton?
the basic precursor of the molecule (L or D glyceraldehyde)
quaternary structure
amphipathic
Ka
32. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
alpha helix
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
isoelectric point
33. Energy storage molecule of carbohydrates for plants
amphoteric
starch
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
maltase
34. Interconversion btw two anomers
mutarotation
glycogen
3 things about the cyclic form of a sugar as a hemiacetal
isoelectric point
35. Hydrolysis
isoelectric point
addition of water across of a bond
glycerol
L- amino acid
36. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
glycogen
tertiary structure
Proteins
triacylglycerol
37. 2 reasons why fats have more efficient energy stores than carbs
has thiol group that allows it the form disulfide bond
cysteine and methionine
packing and energy content
CH3COOH
38. Unique feature of glycine
absolute configuration
only achiral amino acid
the basic precursor of the molecule (L or D glyceraldehyde)
has thiol group that allows it the form disulfide bond
39. Name for 6 membered ring
peptide bonds and disulfide bonds
pyranose
anomeric carbon
glucose - alpha -1 -2- fructose
40. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
1. presence of strong acids 2. proteolytic enzymes
secondary structure
Beta pleated sheet
unsaturated fatty acid
41. Acidic amino acids
glutamic acid and aspartic acid
Proteins
peptide bonds and disulfide bonds
L- configuration
42. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
have an R group that is polar enough to H bond - but does no acts an acid or a base
D- glyceraldehyde
has thiol group that allows it the form disulfide bond
2 things about the cyclic form of a sugar as an acetal
43. 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
antiparallel beta sheet
peptide bond
phospholipids
the basic precursor of the molecule (L or D glyceraldehyde)
44. What configuration do all naturally occuring amino acids have?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
quaternary structure
CH3COOH
L- configuration
45. Sugar with a carbonyl group at the 2 carbon position
have an R group that is polar enough to H bond - but does no acts an acid or a base
Beta pleated sheet
ketose
lactase
46. Basic amino acids
histidine - arginine - lysine
serine - threonine - asparagine - glutamine - cysteine - tyrosine
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
the basic precursor of the molecule (L or D glyceraldehyde)
47. (R) and (S) describe what?
D- amino acid
absolute configuration
lipases
unsaturated fatty acid
48. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
have amino group in their side chains
tertiary structure
will have pI of 6
isomers
49. Formula for urea
absolute configuration
NH2CONH2
have acidic carboxylic acid on side chains - w/ pKa around 4
Ka
50. Glycosidic linkage of lactose
D- glyceraldehyde
amphoteric
anomers
galactose - beta -1 -4- glucose