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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. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Beta pleated sheet
peptide bonds and disulfide bonds
phospholipids
2. Unique feature of glycine
Characteristics of the peptide bond
triacylglycerol
only achiral amino acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
3. What kind of lipids compromise the lipid bilayer?
pyranose
isoelectric point
phospholipids
L- configuration
4. Glyceraldehyde
C3H6O3 - with one chiral center
stereoisomers
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
optical activity
5. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
mutarotation
antiparallel beta sheet
triacylglycerol
only achiral amino acid
6. 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
D- glyceraldehyde
van der Waal forces of hydrophobic tails
peptide bond
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
7. Fatty acid structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
disulfide bond
Characteristics of the peptide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
8. Physiological pH
mutarotation
7.4
L- configuration
amphoteric
9. Sulfur containing amino acids
cysteine and methionine
optical activity
aldose
peptide bond
10. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
ketose
Beta pleated sheet
isomers
primary structure
11. Characteristic of basic amino acids
alpha helix
saturated fatty acid
have amino group in their side chains
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
12. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
Ka
C3H6O3 - with one chiral center
tertiary structure
Proteins
13. Molecules with the same atoms - but different bonds
epimers
isomers
starch
lipases
14. 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)
quaternary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
7.4
epimers
15. Generated btw either thiols on different proteins or thiols on the same protein
disulfide bond
histidine - arginine - lysine
the basic precursor of the molecule (L or D glyceraldehyde)
isomers
16. D and L describe what?
galactose - beta -1 -4- glucose
3 things about the cyclic form of a sugar as a hemiacetal
Cause of Amino acid separation in gel electrophoresis
the basic precursor of the molecule (L or D glyceraldehyde)
17. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
alpha helix
NH2CONH2
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
18. Diastereomers that vary in the configuration of 1 chiral center
have amino group in their side chains
D- amino acid
has thiol group that allows it the form disulfide bond
epimers
19. PH at which the amino acid has a net neutral charge
isoelectric point
C3H6O3 - with one chiral center
Proteins
packing and energy content
20. Acetic acid formula?
stereoisomers
CH3COOH
glucose - alpha -1 -2- fructose
quaternary structure
21. Energy storage molecule of carbohydrates for animals
addition of water across of a bond
peptide bond
glycogen
C3H6O3 - with one chiral center
22. Glycosidic linkage of cellulose
Characteristics of the peptide bond
glucose - beta -1 -4- glucose
has thiol group that allows it the form disulfide bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
23. Energy storage molecule of carbohydrates for plants
glycogen
stereoisomers
starch
furanose
24. Name for 5 membered ring
serine - threonine - asparagine - glutamine - cysteine - tyrosine
has thiol group that allows it the form disulfide bond
furanose
Beta pleated sheet
25. 2 reasons why fats have more efficient energy stores than carbs
alpha helix
phospholipids
packing and energy content
unsaturated fatty acid
26. Naturally occurring carbohydrates are formed from what?
anomers
ketose
furanose
D- glyceraldehyde
27. The amino acid sequence of a protein that is determined by peptide bond
unsaturated fatty acid
galactose - beta -1 -4- glucose
lactase
primary structure
28. Glycosidic linkage of maltose
maltase
peptide bonds and disulfide bonds
glucose - alpha -1 -4- glucose
pI
29. Hydrophilic amino acids
galactose - beta -1 -4- glucose
have acidic carboxylic acid on side chains - w/ pKa around 4
all acidic - basic - and polar amino acids
tertiary structure
30. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
starch
maltase
isomers
secondary structure
31. Fatty acid w/ one or more double bonds in cis form predominately
unsaturated fatty acid
the basic precursor of the molecule (L or D glyceraldehyde)
glycogen
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
32. Unique feature of cysteine
isoelectric point
has thiol group that allows it the form disulfide bond
isomers
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
33. What describes the affinity of functional groups for a proton?
has thiol group that allows it the form disulfide bond
alpha helix
aldose
Ka
34. Characteristics of acidic amino acids
antiparallel beta sheet
histidine - arginine - lysine
have acidic carboxylic acid on side chains - w/ pKa around 4
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
35. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
antiparallel beta sheet
triacylglycerol
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
amphipathic
36. Formula for urea
anomeric carbon
glycogen
NH2CONH2
L- amino acid
37. Basic amino acids
C3H6O3 - with one chiral center
histidine - arginine - lysine
Characteristics of the peptide bond
1. presence of strong acids 2. proteolytic enzymes
38. 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
alpha helix
1. presence of strong acids 2. proteolytic enzymes
anomeric carbon
39. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
anomeric carbon
epimers
Cause of Amino acid separation in gel electrophoresis
have acidic carboxylic acid on side chains - w/ pKa around 4
40. Fatty acid w/ no double bonds and maximum number of hydrogens
NH2CONH2
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
unsaturated fatty acid
saturated fatty acid
41. 2 covalent bonds formed in proteins
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
alpha helix
galactose - beta -1 -4- glucose
peptide bonds and disulfide bonds
42. Name for 6 membered ring
aldose
L- configuration
pyranose
1. presence of strong acids 2. proteolytic enzymes
43. Hydrolysis
addition of water across of a bond
histidine - arginine - lysine
amphoteric
D- glyceraldehyde
44. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
have an R group that is polar enough to H bond - but does no acts an acid or a base
1. presence of strong acids 2. proteolytic enzymes
C3H6O3 - with one chiral center
Beta pleated sheet
45. (R) and (S) describe what?
cysteine and methionine
absolute configuration
isomers
ketose
46. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glucose - alpha -1 -4- glucose
glucose - beta -1 -4- glucose
Beta pleated sheet
47. Amino group placed on the left of a fischer projection is a?
all acidic - basic - and polar amino acids
L- amino acid
addition of water across of a bond
ketose
48. Glycosidic linkage of sucrose
D- amino acid
alpha helix
glucose - alpha -1 -2- fructose
galactose - beta -1 -4- glucose
49. Characteristics of hydrophobic amino acids
all acidic - basic - and polar amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
have amino group in their side chains
CH3COOH
50. Interconversion btw two anomers
lipases
serine - threonine - asparagine - glutamine - cysteine - tyrosine
mutarotation
secondary structure