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