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