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