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