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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. 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
NH2CONH2
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
pyranose
peptide bond
2. (+) and (-) describe what?
unsaturated fatty acid
optical activity
amphipathic
triacylglycerol
3. Enzyme that hydrolyzes maltose into 2 glucose molecules?
anomeric carbon
maltase
epimers
parallel beta sheet
4. Glycosidic linkage of lactose
disulfide bond
pyranose
galactose - beta -1 -4- glucose
NH2CONH2
5. Energy storage molecule of carbohydrates for animals
only amino acid that his a secondary amine
glycogen
parallel beta sheet
amphoteric
6. Characteristics of polar amino acids
glucose - alpha -1 -2- fructose
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
optical activity
have an R group that is polar enough to H bond - but does no acts an acid or a base
7. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
optical activity
antiparallel beta sheet
only amino acid that his a secondary amine
Cause of Amino acid separation in gel electrophoresis
8. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
unsaturated fatty acid
Characteristics of the peptide bond
amphipathic
pyranose
9. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
lipases
1. presence of strong acids 2. proteolytic enzymes
antiparallel beta sheet
glycogen
10. Name for 5 membered ring
alpha helix
saturated fatty acid
absolute configuration
furanose
11. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
galactose - beta -1 -4- glucose
antiparallel beta sheet
CH3COOH
maltase
12. 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
modulates fluidity and seeks to maintain optimal fluidity
alpha helix
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glucose - alpha -1 -2- fructose
13. Amino group placed on the left of a fischer projection is a?
saturated fatty acid
has thiol group that allows it the form disulfide bond
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
L- amino acid
14. Sugar with a carbonyl group at the 2 carbon position
primary structure
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
epimers
ketose
15. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
tertiary structure
van der Waal forces of hydrophobic tails
only achiral amino acid
16. Acidic amino acids
glycogen
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
disulfide bond
glutamic acid and aspartic acid
17. PH at which positive and negative charges balance to form a zwitterion
L- configuration
have an R group that is polar enough to H bond - but does no acts an acid or a base
pI
glucose - alpha -1 -2- fructose
18. Amino group placed on the right of a fischer projection is a?
D- amino acid
glucose - beta -1 -4- glucose
epimers
amphipathic
19. Glyceraldehyde
C3H6O3 - with one chiral center
triacylglycerol
tertiary structure
only achiral amino acid
20. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
parallel beta sheet
histidine - arginine - lysine
saturated fatty acid
alpha helix
21. Fxn of cholesterol in the membrane?
disulfide bond
NH2CONH2
modulates fluidity and seeks to maintain optimal fluidity
7.4
22. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
cysteine and methionine
Proteins
only amino acid that his a secondary amine
will have pI of 6
23. Naturally occurring carbohydrates are formed from what?
glucose - beta -1 -4- glucose
D- glyceraldehyde
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
24. Diastereomers that vary in the configuration of 1 chiral center
peptide bonds and disulfide bonds
glycogen
starch
epimers
25. Glycosidic linkage of maltose
Beta pleated sheet
furanose
absolute configuration
glucose - alpha -1 -4- glucose
26. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
2 things about the cyclic form of a sugar as an acetal
aldose
anomeric carbon
histidine - arginine - lysine
27. What describes the affinity of functional groups for a proton?
only amino acid that his a secondary amine
peptide bonds and disulfide bonds
anomers
Ka
28. Unique feature of proline
CH3COOH
van der Waal forces of hydrophobic tails
only amino acid that his a secondary amine
packing and energy content
29. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
aldose
glycogen
Beta pleated sheet
alpha helix
30. Histidine
quaternary structure
furanose
addition of water across of a bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
31. Basic amino acids
isomers
has thiol group that allows it the form disulfide bond
histidine - arginine - lysine
2 things about the cyclic form of a sugar as an acetal
32. 4 causes of denaturation of proteins
unsaturated fatty acid
Ka
secondary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
33. (R) and (S) describe what?
disulfide bond
absolute configuration
mutarotation
Characteristics of the peptide bond
34. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
peptide bonds and disulfide bonds
lipases
amphipathic
35. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
ketose
Beta pleated sheet
epimers
36. Physiological pH
D- amino acid
maltase
7.4
3 things about the cyclic form of a sugar as a hemiacetal
37. Energy storage molecule of carbohydrates for plants
NH2CONH2
starch
only achiral amino acid
glycogen
38. 3 physiological roles of lipids
quaternary structure
unsaturated fatty acid
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
Ka
39. Characteristics of hydrophobic amino acids
Proteins
starch
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
glucose - beta -1 -4- glucose
40. Nonpolar - hydrophobic amino acids
will have pI of 6
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glucose - alpha -1 -2- fructose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
41. Fatty acid w/ no double bonds and maximum number of hydrogens
the basic precursor of the molecule (L or D glyceraldehyde)
glycerol
saturated fatty acid
glycogen
42. The amino acid sequence of a protein that is determined by peptide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
secondary structure
primary structure
antiparallel beta sheet
43. Fatty acid structure
Ka
absolute configuration
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
has thiol group that allows it the form disulfide bond
44. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
galactose - beta -1 -4- glucose
secondary structure
D- amino acid
45. Name for 6 membered ring
pyranose
L- configuration
cysteine and methionine
have an R group that is polar enough to H bond - but does no acts an acid or a base
46. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
Proteins
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
have amino group in their side chains
47. 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)
anomers
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
quaternary structure
optical activity
48. Sugar with an aldehyde at the first carbon position
anomers
aldose
7.4
3 things about the cyclic form of a sugar as a hemiacetal
49. Glycosidic linkage of cellulose
only achiral amino acid
glucose - beta -1 -4- glucose
triacylglycerol
serine - threonine - asparagine - glutamine - cysteine - tyrosine
50. Unique feature of glycine
have amino group in their side chains
glucose - beta -1 -4- glucose
triacylglycerol
only achiral amino acid