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