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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. 4 causes of denaturation of proteins
mutarotation
aldose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
isoelectric point
2. (+) and (-) describe what?
glucose - alpha -1 -2- fructose
7.4
saturated fatty acid
optical activity
3. Generated btw either thiols on different proteins or thiols on the same protein
van der Waal forces of hydrophobic tails
pI
disulfide bond
7.4
4. 2 covalent bonds formed in proteins
galactose - beta -1 -4- glucose
mutarotation
peptide bonds and disulfide bonds
Cause of Amino acid separation in gel electrophoresis
5. 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
glucose - alpha -1 -4- glucose
Ka
isoelectric point
6. Fxn of cholesterol in the membrane?
isoelectric point
have an R group that is polar enough to H bond - but does no acts an acid or a base
only amino acid that his a secondary amine
modulates fluidity and seeks to maintain optimal fluidity
7. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
D- glyceraldehyde
CH3COOH
isoelectric point
8. Hydrolysis
histidine - arginine - lysine
addition of water across of a bond
primary structure
secondary structure
9. Histidine
has thiol group that allows it the form disulfide bond
L- configuration
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
histidine - arginine - lysine
10. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
amphoteric
Beta pleated sheet
all acidic - basic - and polar amino acids
antiparallel beta sheet
11. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
unsaturated fatty acid
will have pI of 6
packing and energy content
Cause of Amino acid separation in gel electrophoresis
12. Glycosidic linkage of maltose
7.4
serine - threonine - asparagine - glutamine - cysteine - tyrosine
have amino group in their side chains
glucose - alpha -1 -4- glucose
13. 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
glucose - alpha -1 -4- glucose
Proteins
triacylglycerol
14. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
cysteine and methionine
Characteristics of the peptide bond
phospholipids
van der Waal forces of hydrophobic tails
15. Molecules with the same atoms - but different bonds
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
isomers
quaternary structure
will have pI of 6
16. Acetic acid formula?
starch
CH3COOH
aldose
peptide bond
17. 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
galactose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
3 things about the cyclic form of a sugar as a hemiacetal
18. 3 carbon triol that forms backbone of triacylglycerol
anomeric carbon
C3H6O3 - with one chiral center
glycerol
peptide bond
19. Glycosidic linkage of sucrose
glucose - alpha -1 -2- fructose
CH3COOH
NH2CONH2
serine - threonine - asparagine - glutamine - cysteine - tyrosine
20. Sugar with an aldehyde at the first carbon position
mutarotation
secondary structure
aldose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
21. Physiological pH
have an R group that is polar enough to H bond - but does no acts an acid or a base
saturated fatty acid
7.4
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
22. Sugar with a carbonyl group at the 2 carbon position
has thiol group that allows it the form disulfide bond
cysteine and methionine
ketose
antiparallel beta sheet
23. Diastereomers that vary in the configuration of 1 chiral center
quaternary structure
epimers
7.4
glycogen
24. Polar amino acids
aldose
modulates fluidity and seeks to maintain optimal fluidity
serine - threonine - asparagine - glutamine - cysteine - tyrosine
addition of water across of a bond
25. Characteristic of basic amino acids
have an R group that is polar enough to H bond - but does no acts an acid or a base
NH2CONH2
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
have amino group in their side chains
26. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
amphipathic
ketose
unsaturated fatty acid
isoelectric point
27. Glyceraldehyde
C3H6O3 - with one chiral center
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
Characteristics of the peptide bond
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
28. What kind of lipids compromise the lipid bilayer?
7.4
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
phospholipids
starch
29. Fatty acid structure
Proteins
packing and energy content
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
aldose
30. Naturally occurring carbohydrates are formed from what?
glycerol
D- glyceraldehyde
starch
stereoisomers
31. Sulfur containing amino acids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
addition of water across of a bond
1. presence of strong acids 2. proteolytic enzymes
cysteine and methionine
32. The amino acid sequence of a protein that is determined by peptide bond
anomers
anomeric carbon
packing and energy content
primary structure
33. Name for 6 membered ring
pyranose
only amino acid that his a secondary amine
the basic precursor of the molecule (L or D glyceraldehyde)
has thiol group that allows it the form disulfide bond
34. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
parallel beta sheet
glycerol
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
2 things about the cyclic form of a sugar as an acetal
35. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
Ka
only achiral amino acid
aldose
36. Characteristics of polar amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
mutarotation
have an R group that is polar enough to H bond - but does no acts an acid or a base
has thiol group that allows it the form disulfide bond
37. Unique feature of glycine
phospholipids
only achiral amino acid
Characteristics of the peptide bond
tertiary structure
38. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
anomeric carbon
C3H6O3 - with one chiral center
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
peptide bonds and disulfide bonds
39. Enzyme that hydrolyzes maltose into 2 glucose molecules?
aldose
amphipathic
maltase
galactose - beta -1 -4- glucose
40. Molecule can act as a base and as an acid
tertiary structure
maltase
amphoteric
D- amino acid
41. Basic amino acids
histidine - arginine - lysine
amphipathic
galactose - beta -1 -4- glucose
modulates fluidity and seeks to maintain optimal fluidity
42. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
disulfide bond
stereoisomers
the basic precursor of the molecule (L or D glyceraldehyde)
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
43. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
optical activity
will have pI of 6
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
antiparallel beta sheet
44. Amino group placed on the left of a fischer projection is a?
L- amino acid
ketose
glycogen
van der Waal forces of hydrophobic tails
45. Acidic amino acids
amphoteric
glutamic acid and aspartic acid
optical activity
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
46. Enzyme that hydrolyzes lactose into galactose and glucose into
Proteins
lactase
epimers
will have pI of 6
47. Fatty acid w/ one or more double bonds in cis form predominately
3 things about the cyclic form of a sugar as a hemiacetal
cysteine and methionine
pI
unsaturated fatty acid
48. Glycosidic linkage of cellulose
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
phospholipids
van der Waal forces of hydrophobic tails
glucose - beta -1 -4- glucose
49. Energy storage molecule of carbohydrates for plants
L- configuration
will have pI of 6
starch
amphoteric
50. PH at which positive and negative charges balance to form a zwitterion
pI
anomers
the basic precursor of the molecule (L or D glyceraldehyde)
triacylglycerol