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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. Amino group placed on the right of a fischer projection is a?
D- amino acid
isoelectric point
anomers
quaternary structure
2. The amino acid sequence of a protein that is determined by peptide bond
3 things about the cyclic form of a sugar as a hemiacetal
peptide bonds and disulfide bonds
have amino group in their side chains
primary structure
3. Formula for urea
mutarotation
NH2CONH2
absolute configuration
lipases
4. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
1. presence of strong acids 2. proteolytic enzymes
unsaturated fatty acid
furanose
5. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
1. presence of strong acids 2. proteolytic enzymes
secondary structure
2 things about the cyclic form of a sugar as an acetal
ketose
6. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
primary structure
absolute configuration
Characteristics of the peptide bond
cysteine and methionine
7. Generated btw either thiols on different proteins or thiols on the same protein
disulfide bond
Ka
aldose
have acidic carboxylic acid on side chains - w/ pKa around 4
8. 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
Cause of Amino acid separation in gel electrophoresis
alpha helix
NH2CONH2
Beta pleated sheet
9. Physiological pH
Proteins
have amino group in their side chains
the basic precursor of the molecule (L or D glyceraldehyde)
7.4
10. Unique feature of glycine
parallel beta sheet
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
has thiol group that allows it the form disulfide bond
only achiral amino acid
11. Histidine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
parallel beta sheet
only amino acid that his a secondary amine
L- configuration
12. Glycosidic linkage of lactose
tertiary structure
galactose - beta -1 -4- glucose
pyranose
anomeric carbon
13. What kind of lipids compromise the lipid bilayer?
phospholipids
pyranose
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
serine - threonine - asparagine - glutamine - cysteine - tyrosine
14. Diastereomers that vary in the configuration of 1 chiral center
absolute configuration
glutamic acid and aspartic acid
CH3COOH
epimers
15. Energy storage molecule of carbohydrates for plants
glycogen
serine - threonine - asparagine - glutamine - cysteine - tyrosine
starch
ketose
16. Sugar with an aldehyde at the first carbon position
aldose
lipases
have amino group in their side chains
anomers
17. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
phospholipids
addition of water across of a bond
Proteins
18. Acidic amino acids
Beta pleated sheet
antiparallel beta sheet
glutamic acid and aspartic acid
only achiral amino acid
19. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
tertiary structure
D- amino acid
modulates fluidity and seeks to maintain optimal fluidity
will have pI of 6
20. Hydrolysis
van der Waal forces of hydrophobic tails
Proteins
addition of water across of a bond
packing and energy content
21. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
Beta pleated sheet
cysteine and methionine
amphipathic
NH2CONH2
22. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
lipases
maltase
primary structure
23. PH at which positive and negative charges balance to form a zwitterion
addition of water across of a bond
isoelectric point
pI
phospholipids
24. Name for 6 membered ring
phospholipids
pyranose
peptide bonds and disulfide bonds
7.4
25. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
have an R group that is polar enough to H bond - but does no acts an acid or a base
serine - threonine - asparagine - glutamine - cysteine - tyrosine
L- configuration
Proteins
26. Fatty acid w/ one or more double bonds in cis form predominately
glycerol
Ka
van der Waal forces of hydrophobic tails
unsaturated fatty acid
27. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
stereoisomers
packing and energy content
unsaturated fatty acid
28. Hydrophilic amino acids
epimers
isoelectric point
all acidic - basic - and polar amino acids
2 things about the cyclic form of a sugar as an acetal
29. 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
lipases
saturated fatty acid
7.4
30. Molecule can act as a base and as an acid
CH3COOH
amphoteric
only amino acid that his a secondary amine
epimers
31. 3 physiological roles of lipids
epimers
CH3COOH
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
pI
32. Enzyme that hydrolyzes maltose into 2 glucose molecules?
Cause of Amino acid separation in gel electrophoresis
mutarotation
maltase
only amino acid that his a secondary amine
33. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
saturated fatty acid
tertiary structure
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
modulates fluidity and seeks to maintain optimal fluidity
34. 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
1. presence of strong acids 2. proteolytic enzymes
lactase
only amino acid that his a secondary amine
peptide bond
35. Enzymes that hydrolyze fats
lipases
epimers
3 things about the cyclic form of a sugar as a hemiacetal
aldose
36. Energy storage molecule of carbohydrates for animals
glycogen
CH3COOH
L- amino acid
have amino group in their side chains
37. Molecules with the same atoms - but different bonds
isomers
glycerol
epimers
secondary structure
38. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
the basic precursor of the molecule (L or D glyceraldehyde)
stereoisomers
L- amino acid
anomeric carbon
39. (R) and (S) describe what?
amphipathic
the basic precursor of the molecule (L or D glyceraldehyde)
absolute configuration
7.4
40. Naturally occurring carbohydrates are formed from what?
only achiral amino acid
D- glyceraldehyde
parallel beta sheet
3 things about the cyclic form of a sugar as a hemiacetal
41. Name for 5 membered ring
glutamic acid and aspartic acid
2 things about the cyclic form of a sugar as an acetal
furanose
unsaturated fatty acid
42. What stabilizes lipid bilayer?
van der Waal forces of hydrophobic tails
lactase
phospholipids
amphipathic
43. Unique feature of proline
only amino acid that his a secondary amine
L- amino acid
Beta pleated sheet
furanose
44. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
2 things about the cyclic form of a sugar as an acetal
peptide bond
amphipathic
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
45. Epimers of sugars that vary in the configuration of their anomeric carbons
anomers
3 things about the cyclic form of a sugar as a hemiacetal
secondary structure
unsaturated fatty acid
46. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
glucose - beta -1 -4- glucose
only achiral amino acid
2 things about the cyclic form of a sugar as an acetal
triacylglycerol
47. 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
anomers
3 things about the cyclic form of a sugar as a hemiacetal
triacylglycerol
L- amino acid
48. Characteristic of basic amino acids
have amino group in their side chains
peptide bonds and disulfide bonds
have an R group that is polar enough to H bond - but does no acts an acid or a base
aldose
49. Glycosidic linkage of maltose
optical activity
L- configuration
all acidic - basic - and polar amino acids
glucose - alpha -1 -4- glucose
50. Polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
lactase
have an R group that is polar enough to H bond - but does no acts an acid or a base