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