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