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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. Hydrolysis
van der Waal forces of hydrophobic tails
maltase
lipases
addition of water across of a bond
2. Amino group placed on the right of a fischer projection is a?
serine - threonine - asparagine - glutamine - cysteine - tyrosine
only achiral amino acid
CH3COOH
D- amino acid
3. Characteristic of basic amino acids
glucose - beta -1 -4- glucose
disulfide bond
has thiol group that allows it the form disulfide bond
have amino group in their side chains
4. Sulfur containing amino acids
glucose - alpha -1 -2- fructose
cysteine and methionine
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
optical activity
5. Diastereomers that vary in the configuration of 1 chiral center
glycogen
Ka
epimers
L- configuration
6. The amino acid sequence of a protein that is determined by peptide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
primary structure
stereoisomers
antiparallel beta sheet
7. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
phospholipids
ketose
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
8. Acetic acid formula?
amphipathic
primary structure
Characteristics of the peptide bond
CH3COOH
9. Physiological pH
antiparallel beta sheet
pyranose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
7.4
10. Characteristics of hydrophobic amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
histidine - arginine - lysine
1. presence of strong acids 2. proteolytic enzymes
11. Glyceraldehyde
cysteine and methionine
furanose
the basic precursor of the molecule (L or D glyceraldehyde)
C3H6O3 - with one chiral center
12. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
D- glyceraldehyde
L- amino acid
stereoisomers
quaternary structure
13. Name for 5 membered ring
isoelectric point
unsaturated fatty acid
furanose
Characteristics of the peptide bond
14. Enzymes that hydrolyze fats
lipases
ketose
D- amino acid
the basic precursor of the molecule (L or D glyceraldehyde)
15. Sugar with a carbonyl group at the 2 carbon position
amphoteric
disulfide bond
ketose
packing and energy content
16. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
van der Waal forces of hydrophobic tails
glycogen
parallel beta sheet
cysteine and methionine
17. 3 physiological roles of lipids
disulfide bond
parallel beta sheet
packing and energy content
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
18. PH at which the amino acid has a net neutral charge
tertiary structure
maltase
only amino acid that his a secondary amine
isoelectric point
19. (R) and (S) describe what?
ketose
absolute configuration
glucose - beta -1 -4- glucose
Beta pleated sheet
20. Glycosidic linkage of cellulose
7.4
isomers
glucose - beta -1 -4- glucose
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
21. Generated btw either thiols on different proteins or thiols on the same protein
isoelectric point
glucose - beta -1 -4- glucose
absolute configuration
disulfide bond
22. Molecules with the same atoms - but different bonds
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
have amino group in their side chains
L- configuration
isomers
23. What kind of lipids compromise the lipid bilayer?
phospholipids
glycogen
Proteins
glycerol
24. 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)
CH3COOH
furanose
C3H6O3 - with one chiral center
quaternary structure
25. Acidic amino acids
pI
isoelectric point
saturated fatty acid
glutamic acid and aspartic acid
26. Nonpolar - hydrophobic amino acids
triacylglycerol
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
amphipathic
peptide bond
27. Unique feature of cysteine
peptide bonds and disulfide bonds
has thiol group that allows it the form disulfide bond
only amino acid that his a secondary amine
parallel beta sheet
28. Interconversion btw two anomers
pyranose
mutarotation
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
29. What describes the affinity of functional groups for a proton?
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
L- amino acid
Ka
secondary structure
30. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
isoelectric point
antiparallel beta sheet
triacylglycerol
have amino group in their side chains
31. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
stereoisomers
the basic precursor of the molecule (L or D glyceraldehyde)
disulfide bond
32. 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
2 things about the cyclic form of a sugar as an acetal
D- amino acid
amphoteric
33. Naturally occurring carbohydrates are formed from what?
D- glyceraldehyde
glucose - alpha -1 -4- glucose
secondary structure
anomeric carbon
34. Glycosidic linkage of lactose
Proteins
will have pI of 6
galactose - beta -1 -4- glucose
have acidic carboxylic acid on side chains - w/ pKa around 4
35. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
pyranose
van der Waal forces of hydrophobic tails
glucose - beta -1 -4- glucose
36. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
addition of water across of a bond
galactose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
37. Fatty acid structure
NH2CONH2
peptide bond
ketose
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
38. Sugar with an aldehyde at the first carbon position
phospholipids
packing and energy content
absolute configuration
aldose
39. PH at which positive and negative charges balance to form a zwitterion
pI
peptide bond
histidine - arginine - lysine
optical activity
40. Energy storage molecule of carbohydrates for plants
has thiol group that allows it the form disulfide bond
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
glucose - beta -1 -4- glucose
starch
41. Unique feature of proline
anomers
NH2CONH2
primary structure
only amino acid that his a secondary amine
42. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
pyranose
will have pI of 6
modulates fluidity and seeks to maintain optimal fluidity
43. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
Proteins
secondary structure
mutarotation
44. (+) and (-) describe what?
optical activity
isoelectric point
glutamic acid and aspartic acid
aldose
45. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
NH2CONH2
phospholipids
has thiol group that allows it the form disulfide bond
Proteins
46. 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
alpha helix
only achiral amino acid
parallel beta sheet
glutamic acid and aspartic acid
47. Fatty acid w/ no double bonds and maximum number of hydrogens
stereoisomers
will have pI of 6
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
saturated fatty acid
48. 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
peptide bond
absolute configuration
1. presence of strong acids 2. proteolytic enzymes
mutarotation
49. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
3 things about the cyclic form of a sugar as a hemiacetal
starch
stereoisomers
50. Basic amino acids
histidine - arginine - lysine
optical activity
isoelectric point
have acidic carboxylic acid on side chains - w/ pKa around 4