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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. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
anomeric carbon
will have pI of 6
pI
L- configuration
2. Fatty acid w/ one or more double bonds in cis form predominately
isomers
amphipathic
unsaturated fatty acid
aldose
3. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
amphipathic
unsaturated fatty acid
will have pI of 6
tertiary structure
4. What configuration do all naturally occuring amino acids have?
addition of water across of a bond
L- configuration
primary structure
all acidic - basic - and polar amino acids
5. Molecules with the same atoms - but different bonds
isomers
addition of water across of a bond
aldose
modulates fluidity and seeks to maintain optimal fluidity
6. Sulfur containing amino acids
parallel beta sheet
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
cysteine and methionine
CH3COOH
7. Basic amino acids
only amino acid that his a secondary amine
histidine - arginine - lysine
Beta pleated sheet
anomeric carbon
8. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
mutarotation
tertiary structure
have acidic carboxylic acid on side chains - w/ pKa around 4
have amino group in their side chains
9. 3 carbon triol that forms backbone of triacylglycerol
ketose
glycerol
primary structure
glucose - alpha -1 -2- fructose
10. D and L describe what?
pI
the basic precursor of the molecule (L or D glyceraldehyde)
glycerol
saturated fatty acid
11. PH at which the amino acid has a net neutral charge
all acidic - basic - and polar amino acids
alpha helix
D- amino acid
isoelectric point
12. Glycosidic linkage of lactose
7.4
C3H6O3 - with one chiral center
galactose - beta -1 -4- glucose
peptide bonds and disulfide bonds
13. Physiological pH
isoelectric point
peptide bond
7.4
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
14. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
aldose
secondary structure
phospholipids
15. Acidic amino acids
phospholipids
glutamic acid and aspartic acid
only achiral amino acid
the basic precursor of the molecule (L or D glyceraldehyde)
16. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
Proteins
glucose - alpha -1 -2- fructose
1. presence of strong acids 2. proteolytic enzymes
have amino group in their side chains
17. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
optical activity
starch
Characteristics of the peptide bond
secondary structure
18. 4 causes of denaturation of proteins
starch
optical activity
D- amino acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
19. Molecule can act as a base and as an acid
amphoteric
isomers
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
packing and energy content
20. 2 reasons why fats have more efficient energy stores than carbs
Beta pleated sheet
packing and energy content
van der Waal forces of hydrophobic tails
1. presence of strong acids 2. proteolytic enzymes
21. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
CH3COOH
NH2CONH2
antiparallel beta sheet
only amino acid that his a secondary amine
22. What stabilizes lipid bilayer?
disulfide bond
isomers
ketose
van der Waal forces of hydrophobic tails
23. Characteristics of hydrophobic amino acids
furanose
maltase
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
pI
24. Epimers of sugars that vary in the configuration of their anomeric carbons
have amino group in their side chains
primary structure
anomers
mutarotation
25. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
glucose - alpha -1 -4- glucose
starch
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
1. presence of strong acids 2. proteolytic enzymes
26. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
quaternary structure
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
2 things about the cyclic form of a sugar as an acetal
27. Name for 6 membered ring
peptide bond
furanose
stereoisomers
pyranose
28. Sugar with an aldehyde at the first carbon position
aldose
mutarotation
D- glyceraldehyde
D- amino acid
29. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
amphoteric
stereoisomers
peptide bonds and disulfide bonds
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
30. The amino acid sequence of a protein that is determined by peptide bond
lactase
Proteins
primary structure
peptide bond
31. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
packing and energy content
Beta pleated sheet
parallel beta sheet
glutamic acid and aspartic acid
32. Hydrophilic amino acids
2 things about the cyclic form of a sugar as an acetal
Proteins
all acidic - basic - and polar amino acids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
33. 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
alpha helix
histidine - arginine - lysine
CH3COOH
only amino acid that his a secondary amine
34. Formula for urea
NH2CONH2
cysteine and methionine
glutamic acid and aspartic acid
tertiary structure
35. Glycosidic linkage of maltose
primary structure
starch
isomers
glucose - alpha -1 -4- glucose
36. Amino group placed on the left of a fischer projection is a?
1. presence of strong acids 2. proteolytic enzymes
triacylglycerol
quaternary structure
L- amino acid
37. Acetic acid formula?
optical activity
CH3COOH
maltase
glucose - beta -1 -4- glucose
38. Fatty acid structure
glucose - beta -1 -4- glucose
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
L- amino acid
antiparallel beta sheet
39. 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
stereoisomers
isoelectric point
cysteine and methionine
peptide bond
40. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
Cause of Amino acid separation in gel electrophoresis
furanose
amphoteric
7.4
41. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
Proteins
pI
isoelectric point
42. Hydrolysis
addition of water across of a bond
glycerol
glucose - alpha -1 -2- fructose
optical activity
43. Generated btw either thiols on different proteins or thiols on the same protein
peptide bonds and disulfide bonds
unsaturated fatty acid
only achiral amino acid
disulfide bond
44. 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
primary structure
epimers
3 things about the cyclic form of a sugar as a hemiacetal
Proteins
45. Energy storage molecule of carbohydrates for animals
amphoteric
L- configuration
glycogen
maltase
46. Sugar with a carbonyl group at the 2 carbon position
secondary structure
pyranose
lipases
ketose
47. Unique feature of cysteine
modulates fluidity and seeks to maintain optimal fluidity
has thiol group that allows it the form disulfide bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
triacylglycerol
48. 3 physiological roles of lipids
absolute configuration
peptide bond
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
Beta pleated sheet
49. Unique feature of glycine
parallel beta sheet
NH2CONH2
Cause of Amino acid separation in gel electrophoresis
only achiral amino acid
50. Nonpolar - hydrophobic amino acids
CH3COOH
starch
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
amphoteric