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