SUBJECTS
|
BROWSE
|
CAREER CENTER
|
POPULAR
|
JOIN
|
LOGIN
Business Skills
|
Soft Skills
|
Basic Literacy
|
Certifications
About
|
Help
|
Privacy
|
Terms
|
Email
Search
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. PH at which the amino acid has a net neutral charge
quaternary structure
isoelectric point
saturated fatty acid
modulates fluidity and seeks to maintain optimal fluidity
2. Diastereomers that vary in the configuration of 1 chiral center
Beta pleated sheet
amphipathic
epimers
triacylglycerol
3. (+) and (-) describe what?
parallel beta sheet
glucose - alpha -1 -2- fructose
Proteins
optical activity
4. 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
tertiary structure
peptide bond
glucose - alpha -1 -4- glucose
5. Glycosidic linkage of lactose
amphoteric
starch
peptide bond
galactose - beta -1 -4- glucose
6. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
the basic precursor of the molecule (L or D glyceraldehyde)
L- amino acid
only achiral amino acid
1. presence of strong acids 2. proteolytic enzymes
7. What stabilizes lipid bilayer?
the basic precursor of the molecule (L or D glyceraldehyde)
epimers
secondary structure
van der Waal forces of hydrophobic tails
8. Amino group placed on the right of a fischer projection is a?
optical activity
absolute configuration
mutarotation
D- amino acid
9. Generated btw either thiols on different proteins or thiols on the same protein
C3H6O3 - with one chiral center
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
disulfide bond
quaternary structure
10. What configuration do all naturally occuring amino acids have?
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
tertiary structure
L- configuration
11. Formula for urea
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
only amino acid that his a secondary amine
NH2CONH2
7.4
12. Characteristics of acidic amino acids
peptide bond
have acidic carboxylic acid on side chains - w/ pKa around 4
Cause of Amino acid separation in gel electrophoresis
peptide bonds and disulfide bonds
13. Acidic amino acids
triacylglycerol
Beta pleated sheet
glutamic acid and aspartic acid
epimers
14. Glyceraldehyde
disulfide bond
2 things about the cyclic form of a sugar as an acetal
furanose
C3H6O3 - with one chiral center
15. 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
NH2CONH2
has thiol group that allows it the form disulfide bond
lactase
3 things about the cyclic form of a sugar as a hemiacetal
16. What kind of lipids compromise the lipid bilayer?
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
will have pI of 6
phospholipids
absolute configuration
17. Glycosidic linkage of maltose
glucose - alpha -1 -4- glucose
Characteristics of the peptide bond
triacylglycerol
pI
18. 2 covalent bonds formed in proteins
2 things about the cyclic form of a sugar as an acetal
has thiol group that allows it the form disulfide bond
peptide bonds and disulfide bonds
galactose - beta -1 -4- glucose
19. Fatty acid w/ one or more double bonds in cis form predominately
parallel beta sheet
Beta pleated sheet
1. presence of strong acids 2. proteolytic enzymes
unsaturated fatty acid
20. Molecule can act as a base and as an acid
amphoteric
optical activity
epimers
alpha helix
21. Basic amino acids
L- configuration
histidine - arginine - lysine
L- amino acid
C3H6O3 - with one chiral center
22. Acetic acid formula?
amphipathic
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glycerol
CH3COOH
23. 4 causes of denaturation of proteins
tertiary structure
packing and energy content
pI
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
24. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
stereoisomers
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
will have pI of 6
lactase
25. Characteristics of polar amino acids
only achiral amino acid
furanose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
have an R group that is polar enough to H bond - but does no acts an acid or a base
26. Physiological pH
ketose
7.4
furanose
have acidic carboxylic acid on side chains - w/ pKa around 4
27. Sulfur containing amino acids
absolute configuration
stereoisomers
cysteine and methionine
modulates fluidity and seeks to maintain optimal fluidity
28. Glycosidic linkage of sucrose
antiparallel beta sheet
parallel beta sheet
glucose - alpha -1 -2- fructose
mutarotation
29. Hydrolysis
ketose
peptide bonds and disulfide bonds
addition of water across of a bond
starch
30. Histidine
glycerol
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glucose - alpha -1 -2- fructose
31. Fatty acid structure
optical activity
histidine - arginine - lysine
serine - threonine - asparagine - glutamine - cysteine - tyrosine
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
32. Characteristics of hydrophobic amino acids
packing and energy content
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
starch
Ka
33. Nonpolar - hydrophobic amino acids
pI
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
serine - threonine - asparagine - glutamine - cysteine - tyrosine
stereoisomers
34. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
ketose
furanose
Beta pleated sheet
35. (R) and (S) describe what?
glucose - alpha -1 -4- glucose
2 things about the cyclic form of a sugar as an acetal
galactose - beta -1 -4- glucose
absolute configuration
36. Fatty acid w/ no double bonds and maximum number of hydrogens
saturated fatty acid
only achiral amino acid
amphoteric
secondary structure
37. D and L describe what?
maltase
the basic precursor of the molecule (L or D glyceraldehyde)
peptide bond
lipases
38. Enzyme that hydrolyzes maltose into 2 glucose molecules?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
maltase
lactase
unsaturated fatty acid
39. PH at which positive and negative charges balance to form a zwitterion
2 things about the cyclic form of a sugar as an acetal
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
unsaturated fatty acid
pI
40. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
CH3COOH
triacylglycerol
C3H6O3 - with one chiral center
will have pI of 6
41. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
phospholipids
D- amino acid
2 things about the cyclic form of a sugar as an acetal
anomers
42. Sugar with a carbonyl group at the 2 carbon position
ketose
modulates fluidity and seeks to maintain optimal fluidity
serine - threonine - asparagine - glutamine - cysteine - tyrosine
Beta pleated sheet
43. What describes the affinity of functional groups for a proton?
L- amino acid
Ka
pyranose
L- configuration
44. Unique feature of proline
only amino acid that his a secondary amine
has thiol group that allows it the form disulfide bond
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
starch
45. 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
addition of water across of a bond
Proteins
Cause of Amino acid separation in gel electrophoresis
46. Enzymes that hydrolyze fats
serine - threonine - asparagine - glutamine - cysteine - tyrosine
lipases
unsaturated fatty acid
isoelectric point
47. 2 reasons why fats have more efficient energy stores than carbs
isomers
have amino group in their side chains
packing and energy content
isoelectric point
48. Energy storage molecule of carbohydrates for animals
Beta pleated sheet
histidine - arginine - lysine
cysteine and methionine
glycogen
49. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
amphipathic
3 things about the cyclic form of a sugar as a hemiacetal
histidine - arginine - lysine
saturated fatty acid
50. 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
D- glyceraldehyde
peptide bond
Cause of Amino acid separation in gel electrophoresis
parallel beta sheet