SUBJECTS
|
BROWSE
|
CAREER CENTER
|
POPULAR
|
JOIN
|
LOGIN
Business Skills
|
Soft Skills
|
Basic Literacy
|
Certifications
About
|
Help
|
Privacy
|
Terms
|
Email
Search
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. Naturally occurring carbohydrates are formed from what?
all acidic - basic - and polar amino acids
C3H6O3 - with one chiral center
D- glyceraldehyde
glutamic acid and aspartic acid
2. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
glucose - alpha -1 -4- glucose
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
CH3COOH
3. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
pyranose
galactose - beta -1 -4- glucose
mutarotation
secondary structure
4. What configuration do all naturally occuring amino acids have?
peptide bonds and disulfide bonds
L- configuration
pI
7.4
5. Unique feature of proline
only amino acid that his a secondary amine
Ka
tertiary structure
lactase
6. 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
3 things about the cyclic form of a sugar as a hemiacetal
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
L- configuration
lipases
7. Fatty acid w/ one or more double bonds in cis form predominately
has thiol group that allows it the form disulfide bond
unsaturated fatty acid
Beta pleated sheet
anomeric carbon
8. Amino group placed on the left of a fischer projection is a?
1. presence of strong acids 2. proteolytic enzymes
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
Characteristics of the peptide bond
L- amino acid
9. 2 covalent bonds formed in proteins
maltase
antiparallel beta sheet
all acidic - basic - and polar amino acids
peptide bonds and disulfide bonds
10. Characteristics of acidic amino acids
ketose
have acidic carboxylic acid on side chains - w/ pKa around 4
modulates fluidity and seeks to maintain optimal fluidity
peptide bonds and disulfide bonds
11. Glycosidic linkage of cellulose
glucose - beta -1 -4- glucose
peptide bond
only amino acid that his a secondary amine
van der Waal forces of hydrophobic tails
12. Diastereomers that vary in the configuration of 1 chiral center
epimers
all acidic - basic - and polar amino acids
Cause of Amino acid separation in gel electrophoresis
NH2CONH2
13. Glycosidic linkage of lactose
Beta pleated sheet
CH3COOH
galactose - beta -1 -4- glucose
ketose
14. PH at which the amino acid has a net neutral charge
glutamic acid and aspartic acid
isoelectric point
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Ka
15. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
stereoisomers
will have pI of 6
glucose - alpha -1 -4- glucose
packing and energy content
16. Sugar with a carbonyl group at the 2 carbon position
L- configuration
ketose
2 things about the cyclic form of a sugar as an acetal
amphoteric
17. Polar amino acids
CH3COOH
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
glucose - alpha -1 -4- glucose
18. Unique feature of glycine
have amino group in their side chains
optical activity
only achiral amino acid
alpha helix
19. Glyceraldehyde
isomers
C3H6O3 - with one chiral center
Cause of Amino acid separation in gel electrophoresis
tertiary structure
20. 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
NH2CONH2
alpha helix
disulfide bond
starch
21. 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
peptide bond
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glucose - alpha -1 -2- fructose
addition of water across of a bond
22. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
cysteine and methionine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
stereoisomers
triacylglycerol
23. Hydrophilic amino acids
all acidic - basic - and polar amino acids
1. presence of strong acids 2. proteolytic enzymes
epimers
Ka
24. 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
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
optical activity
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
25. 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
peptide bond
L- configuration
will have pI of 6
26. Fxn of cholesterol in the membrane?
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
glucose - alpha -1 -4- glucose
modulates fluidity and seeks to maintain optimal fluidity
have acidic carboxylic acid on side chains - w/ pKa around 4
27. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
maltase
anomeric carbon
28. Nonpolar - hydrophobic amino acids
NH2CONH2
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
anomeric carbon
29. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
anomers
Proteins
stereoisomers
antiparallel beta sheet
30. (+) and (-) describe what?
optical activity
peptide bonds and disulfide bonds
parallel beta sheet
saturated fatty acid
31. Fatty acid structure
only achiral amino acid
NH2CONH2
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
CH3COOH
32. Generated btw either thiols on different proteins or thiols on the same protein
have amino group in their side chains
modulates fluidity and seeks to maintain optimal fluidity
disulfide bond
histidine - arginine - lysine
33. Enzymes that hydrolyze fats
lipases
quaternary structure
NH2CONH2
unsaturated fatty acid
34. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
C3H6O3 - with one chiral center
anomeric carbon
CH3COOH
has thiol group that allows it the form disulfide bond
35. Amino group placed on the right of a fischer projection is a?
L- configuration
1. presence of strong acids 2. proteolytic enzymes
D- amino acid
CH3COOH
36. Sulfur containing amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
saturated fatty acid
glycerol
cysteine and methionine
37. Molecule can act as a base and as an acid
have acidic carboxylic acid on side chains - w/ pKa around 4
1. presence of strong acids 2. proteolytic enzymes
CH3COOH
amphoteric
38. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
all acidic - basic - and polar amino acids
parallel beta sheet
disulfide bond
amphipathic
39. Glycosidic linkage of maltose
isomers
primary structure
glucose - alpha -1 -4- glucose
van der Waal forces of hydrophobic tails
40. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
parallel beta sheet
1. presence of strong acids 2. proteolytic enzymes
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
lactase
41. 3 carbon triol that forms backbone of triacylglycerol
saturated fatty acid
glycerol
disulfide bond
isoelectric point
42. Molecules with the same atoms - but different bonds
antiparallel beta sheet
isomers
amphipathic
have acidic carboxylic acid on side chains - w/ pKa around 4
43. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
stereoisomers
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
lipases
secondary structure
44. Basic amino acids
peptide bond
all acidic - basic - and polar amino acids
histidine - arginine - lysine
tertiary structure
45. Fatty acid w/ no double bonds and maximum number of hydrogens
amphoteric
saturated fatty acid
glucose - alpha -1 -4- glucose
Proteins
46. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
Ka
Cause of Amino acid separation in gel electrophoresis
2 things about the cyclic form of a sugar as an acetal
47. Formula for urea
galactose - beta -1 -4- glucose
mutarotation
NH2CONH2
amphoteric
48. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
L- configuration
D- amino acid
ketose
1. presence of strong acids 2. proteolytic enzymes
49. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
anomeric carbon
lactase
D- glyceraldehyde
50. What describes the affinity of functional groups for a proton?
have acidic carboxylic acid on side chains - w/ pKa around 4
Ka
optical activity
histidine - arginine - lysine