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