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