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