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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
optical activity
L- configuration
Proteins
2. Fatty acid w/ one or more double bonds in cis form predominately
Proteins
unsaturated fatty acid
amphoteric
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
3. Amino group placed on the right of a fischer projection is a?
maltase
epimers
D- amino acid
galactose - beta -1 -4- glucose
4. (R) and (S) describe what?
galactose - beta -1 -4- glucose
glycerol
absolute configuration
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
5. Sulfur containing amino acids
pI
amphipathic
secondary structure
cysteine and methionine
6. Enzyme that hydrolyzes lactose into galactose and glucose into
will have pI of 6
optical activity
histidine - arginine - lysine
lactase
7. 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
the basic precursor of the molecule (L or D glyceraldehyde)
peptide bond
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
D- glyceraldehyde
8. Epimers of sugars that vary in the configuration of their anomeric carbons
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glutamic acid and aspartic acid
anomers
furanose
9. (+) and (-) describe what?
glycerol
have an R group that is polar enough to H bond - but does no acts an acid or a base
optical activity
antiparallel beta sheet
10. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
alpha helix
have amino group in their side chains
stereoisomers
antiparallel beta sheet
11. Fatty acid w/ no double bonds and maximum number of hydrogens
amphipathic
saturated fatty acid
all acidic - basic - and polar amino acids
tertiary structure
12. Hydrolysis
addition of water across of a bond
anomeric carbon
Ka
anomers
13. 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
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
alpha helix
peptide bond
packing and energy content
14. The amino acid sequence of a protein that is determined by peptide bond
primary structure
isomers
amphipathic
galactose - beta -1 -4- glucose
15. Generated btw either thiols on different proteins or thiols on the same protein
disulfide bond
NH2CONH2
unsaturated fatty acid
mutarotation
16. Glycosidic linkage of cellulose
has thiol group that allows it the form disulfide bond
triacylglycerol
glucose - beta -1 -4- glucose
have acidic carboxylic acid on side chains - w/ pKa around 4
17. Interconversion btw two anomers
mutarotation
optical activity
serine - threonine - asparagine - glutamine - cysteine - tyrosine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
18. Energy storage molecule of carbohydrates for animals
glycogen
stereoisomers
has thiol group that allows it the form disulfide bond
Proteins
19. Name for 5 membered ring
optical activity
Characteristics of the peptide bond
furanose
anomers
20. Unique feature of proline
only amino acid that his a secondary amine
phospholipids
maltase
secondary structure
21. Glycosidic linkage of maltose
glucose - alpha -1 -4- glucose
L- amino acid
Ka
all acidic - basic - and polar amino acids
22. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
maltase
cysteine and methionine
secondary structure
saturated fatty acid
23. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
have acidic carboxylic acid on side chains - w/ pKa around 4
ketose
stereoisomers
glucose - alpha -1 -2- fructose
24. What configuration do all naturally occuring amino acids have?
L- configuration
alpha helix
modulates fluidity and seeks to maintain optimal fluidity
D- amino acid
25. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
secondary structure
disulfide bond
2 things about the cyclic form of a sugar as an acetal
will have pI of 6
26. Sugar with a carbonyl group at the 2 carbon position
histidine - arginine - lysine
ketose
saturated fatty acid
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
27. Naturally occurring carbohydrates are formed from what?
unsaturated fatty acid
D- glyceraldehyde
absolute configuration
2 things about the cyclic form of a sugar as an acetal
28. PH at which positive and negative charges balance to form a zwitterion
glucose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
the basic precursor of the molecule (L or D glyceraldehyde)
pI
29. 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)
disulfide bond
modulates fluidity and seeks to maintain optimal fluidity
van der Waal forces of hydrophobic tails
quaternary structure
30. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
tertiary structure
isoelectric point
Characteristics of the peptide bond
31. Acetic acid formula?
2 things about the cyclic form of a sugar as an acetal
Characteristics of the peptide bond
CH3COOH
D- glyceraldehyde
32. Characteristics of polar amino acids
galactose - beta -1 -4- glucose
amphipathic
Proteins
have an R group that is polar enough to H bond - but does no acts an acid or a base
33. Formula for urea
pyranose
peptide bond
NH2CONH2
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
34. Glycosidic linkage of sucrose
D- amino acid
C3H6O3 - with one chiral center
Ka
glucose - alpha -1 -2- fructose
35. Characteristics of acidic amino acids
aldose
van der Waal forces of hydrophobic tails
only amino acid that his a secondary amine
have acidic carboxylic acid on side chains - w/ pKa around 4
36. Molecule can act as a base and as an acid
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
amphoteric
disulfide bond
37. Fxn of cholesterol in the membrane?
cysteine and methionine
modulates fluidity and seeks to maintain optimal fluidity
isomers
D- glyceraldehyde
38. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
mutarotation
isoelectric point
has thiol group that allows it the form disulfide bond
tertiary structure
39. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
secondary structure
have amino group in their side chains
modulates fluidity and seeks to maintain optimal fluidity
amphipathic
40. Characteristics of hydrophobic amino acids
ketose
3 things about the cyclic form of a sugar as a hemiacetal
secondary structure
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
41. What describes the affinity of functional groups for a proton?
glucose - alpha -1 -4- glucose
Ka
starch
modulates fluidity and seeks to maintain optimal fluidity
42. 2 covalent bonds formed in proteins
anomers
only amino acid that his a secondary amine
peptide bonds and disulfide bonds
mutarotation
43. Diastereomers that vary in the configuration of 1 chiral center
anomeric carbon
1. presence of strong acids 2. proteolytic enzymes
epimers
optical activity
44. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
will have pI of 6
mutarotation
Proteins
2 things about the cyclic form of a sugar as an acetal
45. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
alpha helix
glycogen
Cause of Amino acid separation in gel electrophoresis
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
46. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
2 things about the cyclic form of a sugar as an acetal
alpha helix
peptide bonds and disulfide bonds
Characteristics of the peptide bond
47. Molecules with the same atoms - but different bonds
peptide bonds and disulfide bonds
disulfide bond
van der Waal forces of hydrophobic tails
isomers
48. PH at which the amino acid has a net neutral charge
only achiral amino acid
lipases
isoelectric point
glycogen
49. D and L describe what?
glucose - alpha -1 -2- fructose
quaternary structure
the basic precursor of the molecule (L or D glyceraldehyde)
disulfide bond
50. Name for 6 membered ring
primary structure
pyranose
1. presence of strong acids 2. proteolytic enzymes
secondary structure