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Biochemistry I Module of the MCAT Self Prep eCourse: Lesson 1: Amino Acids and Proteins (Pro)

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Lesson 1: Amino Acids and Proteins
Lesson 1: Amino Acids and Proteins
What are the building blocks of DNA/RNA? Protein?
DNA/RNA are made up of nucleotides.
Protein is made up of amino acids.
Which process is when DNA copies itself?

(A) Replication
(B) Translation
(C) Transcription
(D) Integration
(A) Replication

DNA is restored as DNA when it copies itself during "replication."
Which process is when DNA is copied into RNA?

(A) Replication
(B) Translation
(C) Transcription
(D) Integration
(C) Transcription

DNA is copied into RNA in a process called "transcription."
Which process is when RNA is used to synthesize a protein?

(A) Replication
(B) Translation
(C) Transcription
(D) Integration
(B) Translation

RNA is used to synthesize a protein in "translation."
Compare and contrast replication and synthesis.
In both replication and synthesis, single stranded DNA is used as a template to make another polymer.
In replication, that DNA is used to make another DNA strand, resulting in two copies of the DNA. This is useful before mitosis.
In synthesis, DNA is translated into RNA, which can then be used for protein synthesis later on.
What is the difference between Polymers and Monomers?
Polymers are made up of individual sub-units called monomers.
True or False? DNA, RNA, and protein are all linear polymers.
True. The structure of DNA, RNA, and protein is similar in that they are all linear polymers because each individual unit (or monomer) is attached to only one or two other units, resulting in a long chain.
What are the monomers called for DNA and RNA? Protein?
The monomers in DNA and RNA are nucleotides.

The monomers in protein are called amino acids.
Why is it important that DNA, RNA, and protein have the same linear polymer structure?
Its important that DNA, RNA, and protein have the same linear polymer structure because this helps to transfer and preserve the encoding of information during transcription and translation.
What is the central dogma of molecular biology?
DNA makes RNA makes protein.
In order to build single stranded DNA, each nucleic acid can only be attached to (at most) how many other nucleic acids?

(A) 1
(B) 2
(C) 3
(D) 4
(B) 2

In order to build single stranded DNA, each nucleic acid can only be attached to two other nucleic acids, one on the left and one on the right.
How can one easily differentiate transcription and translation using base words "script" and "translate"?
The word "script" refers to written forms. Transcription goes from one written form (DNA) to another (RNA) using a common "alphabet" aka nucleic acids.

Translation refers to the need to "translate" from one language to another. Here, nucleic acids from one language (RNA) are translated into amino acids of another language (protein).
What is the term for when information flows backward from RNA to DNA?
Reverse transcription
What is the function of reverse transcriptase?
Reverse transcriptase carries out reverse transcription, in which complementary DNA (cDNA) is generated from an RNA template.
What is most likely to happen if a patient with the retrovirus HIV is administered a medicinal drug that deactivates the enzyme reverse transcriptase?

(A) The patient will die.
(B) The patient's chances at survival will increase.
(C) The patient's chances at survival will decrease, but they will not die.
(D) The patient may go into a coma.
(B) The patient's chances at survival will increase.

Since reverse transcriptase transcribes the retrovirus RNA back into DNA, deactivating reverse transcriptase will halt HIV retrovirus replication and integration into the host genome. This will be a somewhat effective treatment against HIV!
True or False? RNA viruses, such as coronavirus, influenza virus, and paramyxovirus viruses, can have their genetic material translated immediately by host cell machinery as compared with DNA viruses and retroviruses.
True. RNA viruses have their genetic material stored as RNA (as opposed to DNA), so their genome can directly use host cell replication machinery, as if it were messenger RNA. This means RNA viruses can have their proteins produced directly.
Which of the following are examples of non-coding RNA (ncRNA)? Why are they called that?

I. tRNA
II. mRNA
III. rRNA

(A) I Only
(B) II Only
(C) I and II Only
(D) I and III Only
(D) I and III Only

Transfer RNA (tRNA) and Ribosomal RNA (rRNA) are both examples of non-coding RNA (ncRNA) because they are not translated into a protein themselves, but rather perform functions during the process of translation by helping messenger RNA (mRNA) create proteins.
What are the primary functions of transfer RNA (tRNA) and ribosomal RNA (rRNA)?
Transfer RNA (tRNA) carries amino acids to the ribosome and acts as a "bridge" by matching a codon in mRNA with its corresponding amino acid.

Ribosomal RNA (rRNA) is responsible for the structure and function of the ribosome.
Do the discoveries of reverse transcription, RNA viruses and noncoding RNA support or violate the central dogma?
These discoveries violate the central dogma. These are processes that use other mechanisms than, or run counter to the central dogma.
What is the result of methylating p53? Why is this considered an example of epigenetics?
When p53, a tumor suppressor gene, is methylated, p53 gene expression is turned off, leading to the progression of cancer cells. This change in gene activity is called epigenetics because DNA expression is modified due to methylation (turning "off" a gene expression), or demethylation (turning "on" a gene expression), which is a modification of DNA expression without affecting the DNA sequence.
How can a cell in your muscle have the same DNA as a cell in your skin when they are completely different from one another in terms of cell function?
It is because epigenetic mechanisms allow the transcription of only certain genes within the genome which changes the way each cell behaves. The DNA is the same, but the modifications of the DNA are different, leading to different gene expression.
Peptide bonds are a special kind of link between which type of monomers?

(A) Monosaccharides
(B) Amino Acids
(C) Nucleic Acids
(D) Monopeptides
(B) Amino Acids

Amino acids are linked together through bonds called peptide bonds.
Draw the structure of an amino acid. Circle the alpha carbon.
Peptide bonds are formed via what mechanism? Explain or draw out this mechanism.

(A) Hydration
(B) Hydrolysis
(C) Condensation
(D) Oxidation-reduction
(C) Condensation

Peptide bonds are formed by the nucleophilic addition-elimination reaction, which is a type of condensation reaction. The electron pair on the amino group of one amino acid will nucleophilically attack the carbonyl carbon of the carboxyl group of another amino acid, releasing a water molecule and forming an amide or "peptide" bond.
Draw out the resonance structures that result in a peptide bond.
The peptide bond resonance structure shares electrons between the oxygen and nitrogen atoms.
The resonance structure of the peptide bond has a double bond character. Which of the following correctly describe the peptide bond?

I. Rigid
II. Planar
III. Does not rotate

(A) I Only
(B) I and II Only
(C) II and III Only
(D) I, II, and III
(D) I, II, and III

Since there is double bond character in a peptide bond, the peptide bond is very rigid, planar, and does not rotate.

However, do not confuse the rigidity of the peptide bond with the entire polypeptide structure. Remember that alpha carbon atoms freely rotate on each amino acid.
What does the N-terminal refer to compared the C-terminal?
The N-terminal is where synthesis of a polypeptide begins. There is a free amino group at this end of the polypeptide chain.

The C-terminal is where synthesis of a polypeptide ends. There is a free carboxyl group at this end of the polypeptide chain.
What does hydrolysis do to a peptide bond?
Hydrolysis uses water as a reactant to break peptide bonds with the help of either strong acids or proteolytic enzymes.
What is the difference between acid hydrolysis and proteolysis when breaking a peptide bond?
Acid Hydrolysis: Breaks/cleaves a peptide bond in a non-specific way and requires acid and heat.

Proteolysis: Breaks/cleaves specific peptide bonds within the polypeptide chain.
An enzyme called Trypsin produced in the pancreas cleaves the carboxyl end of either arginine or lysine. Would this be considered acid hydrolysis or proteolysis? Why?
Proteolytic cleavage (proteolysis) because Trypsin cleaves at a specific peptide bond terminal (C terminal).
Which amino acid is most likely to be found at the active site of an enzyme? Why?

(A) His
(B) Pro
(C) Gly
(D) Cys
(A) His

Histidine, because its side chain has a pKa (6.5) roughly equal to physiological pH (7.4) thus allowing histidine to exist in both its protonated and deprotonated form to stabilize/destabilize a substrate in an enzyme catalysis process.

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Would Histidine's R Group be protonated or deprotonated at a pH of 4.0?
Protonated because the pH (4.0) < pKa (6.5)

pH < pKa then the amino acid will be in its protonated form.
pH > pKa then the amino acid will be in its deprotonated form.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Looking under a microscope, you see that there is a disruption in the pattern of protein structure. Which amino acid(s) is/are likely responsible for this pattern of disruption?

I. R
II. G
III. P

(A) I Only
(B) II and III Only
(C) I and III Only
(D) I, II, and III
(B) II and III Only

Proline and glycine are likely to attribute to disruption in protein structure because proline has a secondary alpha amino group as part of its side chain; thus, introducing a kink. Glycine has a hydrogen atom as its side chain, making it very small and flexible. Remember: glycine & proline = "alpha helix breakers."

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
A scientist puts a protein structure under plane polarized light. Which amino acid will not show optical activity?

(A) Thr
(B) Arg
(C) Gly
(D) Glu
(C) Gly

Glycine is the only amino acid that does not rotate the plane of plane-polarized light because glycine is an achiral compound, making it optically inactive.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Which amino acid is able to form disulfide bridges within a polypeptide chain or between two different polypeptide chains?

(A) Phe
(B) Cys
(C) Gln
(D) Met
(B) Cys

Cysteine is able to form disulfide bridges within a polypeptide chain or between two different polypeptide chains.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What happens to the structure of cysteine when it goes from the intracellular to the extracellular space?
As cysteine goes from its reduced form in intracellular environments to its oxidized form in extracellular space. In its oxidized form, it can form the disulfide bridges!

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
An unknown, rare disease causes a breakdown of polypeptide chains by disrupting its tertiary and quarternary structure. Which amino acid is likely involved? Why?

(A) His
(B) Pro
(C) Gly
(D) Cys
(D) Cys

The pathology of the disease is most likely affecting the amino acid cysteine's ability to form disulfide bridges in an oxidized environment (which typically favors the formation of disulfide bridges).

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What 4 groups are attached to the central carbon of an amino acid?
An amino acid has an amino group, a carboxylic acid group, a hydrogen atom, and a R side chain.
What does the alpha carbon refer to?
The alpha carbon is referred to as the carbon adjacent to the carboxylic acid carbon.
What does the chiral carbon refer to?
Chiral carbon means that the alpha carbon has 4 different substituents. It also means it is optically active meaning that it can rotate light.
Which amino acid does not have a chiral carbon?

(A) His
(B) Pro
(C) Gly
(D) Cys
(C) Gly

Glycine is the only amino acid that does not have a chiral carbon.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the difference between L-amino acid and D-amino acid?
L-amino acid has an amino group shown on the left side in a Fischer projection while the D-amino acid has an amino group shown on the right side of a Fischer projection.
What makes a molecule considered an enantiomer?
Enantiomers are mirror-image molecules that are not superimposable.
Which form of amino acids, L- or D-amino acids, is found in the human body?
L-amino acids are the only form that will be found in the human body.
What is the isoelectronic point of an amino acid?
Isoelectric Point is the pH at which an amino acid exists in a neutral form with zero charge.
What is the pKa of the amino group of an Amino Acid?

(A) 2
(B) 6
(C) 9
(D) 12
(C) 9

The amino group on the amino acid is a proton acceptor, making it basic with a pKa around 9;

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the pKa of the carboxylic acid group of an Amino Acid?

(A) 2
(B) 6
(C) 9
(D) 12
(A) 2

The carboxylic group of the amino acid is a proton donor, making it acidic with a pKa around 2.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the difference between the zwitterionic and non-zwitterionic form of an amino acid?
An amino acid with both a negative charge and a positive charge present on the carboxylic acid group and amino group, respectively, is called a zwitterion.

It's non-zwitterionic form occurs when both groups have no charge.
When will an amino acid be fully protonated vs. deprotonated?
At low pH the amino acid will be fully protonated with a positive net charge. At high pH, the amino acid will be fully deprotonated with a negative net charge.
What is the pKa of the R group for Asp? Glu? His? Cys? Tyr? Lys? Arg?
Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
How do you calculate the isoelectric point of an amino acid?
The pI for a simple compound can be calculated by averaging
the 2 pKa's that are relevant to the concentration of the
molecule in its neutral charge state.

Neutral R group: the pI is the average of the C- and N- terminus pKa values.
Acidic R group: the pI is the average of the C-terminus and side chain
Basic R group: the pI is the average of the N-terminus and side chain

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What is the isoelectronic point for glutamic acid with α-carboxyl (α-COOH, pK1 = 2.19), α-amino (α-NH3+, pK2 = 9.67), and R-group carboxyl (R-COOH, pKR = 4.25)?

(A) 2.19
(B) 3.22
(C) 6.02
(D) 7.45
(B) 3.22

Because glutamic acid has an acidic R-group, the pI can be calculated by averaging of the C-terminus and R-group side chain. Thus, (( α-COOH, pK1 = 2.19)+(R-COOH, pKR = 4.25))/2= 3.22.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Which amino acid would you expect to find facing the lipid bilayer in an integral membrane protein?

(A) D
(B) Y
(C) R
(D) L
(D) L (Leucine)

You would expect to find hydrophobic (nonpolar) amino acids, such as amino acids with alkyl and aromatic rings as their side chains.

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Which amino acid would you expect to find on the surface of a soluble protein?

(A) E
(B) I
(C) P
(D) F
(A) E (Glutamate)

You would expect to find polar, hydrophilic amino acids with side chains containing O, S or N atoms.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Acidic, polar amino acids have R groups containing which functional group?

(A) Hydroxyl
(B) Carboxyl
(C) Amino
(D) Thiol
(B) Carboxyl

Acidic amino acid R-groups contain carboxylic acids as seen in Aspartic and Glutamic acid.

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What functional groups do the R-groups of neutral, polar amino acids have that the R-groups of neutral, non-polar amino acids do not?

I. Thiol
II. Hydroxy
III. Amide

(A) I Only
(B) III Only
(C) I and II Only
(D) I, II, and III
(D) I, II, and III

Neutral polar amino acids often contain O (Hydroxy Groups) or S atoms (Thiol Groups) or Amide groups (Carboxylic Acid derivative with an Amino group). Neutral, non polar amino acids contain uncharged, alkyl or aromatic side chains.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Which bond stabilizes the primary structure of a protein?

(A) Hydrogen Bonds
(B) Covalent Bonds
(C) Van Der Waals Forces
(D) Dipole-dipole Interactions
(B) Covalent Bonds

The primary structure describes the linear sequence of amino acids stabilized by peptide bonds.

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Which bond stabilizes the secondary structure of a protein?

(A) Hydrogen Bonds
(B) Covalent Bonds
(C) Van Der Waals Forces
(D) Dipole-dipole Interactions
(A) Hydrogen Bonds

The secondary structure of a protein is referred to as the way that a linear sequence of amino acids folds upon itself, such as an alpha helix or beta sheet. Secondary structure is stabilized by hydrogen bonds.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the tertiary structure of a protein?
Tertiary structure refers to a higher order of folding within a polypeptide chain or the many different folds within a polypeptide. It depends on distant group interactions.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Which side of a cell membrane would one find disulfide bonds?

(A) Extracellular
(B) Intracellular
(C) Within the cell membrane
(D) In the Nucleus
(A) Extracellular

Disulfide bonds are found in the extracellular space which facilitates an oxidative environment.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Why would the extracellular space facilitate an oxidative environment whereas intracellular space does not?
Cells contain many antioxidants to protect from oxidative damage to important structures, creating a reducing environment inside the cell. The extracellular space does not have these same antioxidants.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
The tertiary structure of a protein and quaternary structure of a protein are similar in that they are stabilized by the same interactions, which include:

I. Hydrogen Bonding
II. Disulfide Bonds
III. Hydrophobic Interactions

(A) I Only
(B) III Only
(C) I and II Only
(D) I, II, and III
(D) I, II, and III

The tertiary and quaternary structure of a protein are both stabilized by the same type of interactions, which are:
-hydrogen bonding
-Van der Waals forces
-disulfide bonding
-hydrophobic interactions

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the quaternary structure of a protein?
Quaternary structure of the protein refers to the bonding/interaction of multiple polypeptides. Each polypeptide is called a subunit. For instance, 2 subunits = dimer, 3 subunits = trimer, 4 subunits = tetramer, >4 subunits = multimer.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the difference between a conformational protein vs. a denatured protein?
Conformational protein refers to the protein's folded 3D structure in its an active form.

Denatured protein means the protein has become unfolded and is in an inactive form.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is the "solvation shell"? What is its role?
A solvation shell is the layer of solvent that surrounds a protein. An example of a solvation shell is when the partially-negative oxygen atoms of water molecules surround positively charged amino acid residues on the exterior surface of a protein, thus stabilizing the conformation of this protein.

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If you denature a protein by adding heat, all different levels of protein structure will be destroyed except for which level? Why?

(A) Primary Structure
(B) Secondary Structure
(C) Tertiary Structure
(D) Quarternary Structure
(A) Primary Structure

Primary structure because peptide bonds are not broken simply due to heat.

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What method is best if you want to break only the ionic bonds in protein? Which levels of protein structure will be affected?

I. Secondary Structure
II. Tertiary Structure
III. Quarternary Structure

(A) I Only
(B) III Only
(C) II and III Only
(D) I, II, and III
(C) II and III Only

Changing the pH surrounding the protein will disrupt all ionic bonds in a protein, which mainly denature tertiary and quaternary structure of a protein.

Keep in mind that the Hydrogen Bonds are formed between the Carboxy group and the Amino Group. When these are part of a peptide chain, it would take a very large change in pH to deprotonate or protonate them.

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How would a chemical denaturant affect proteins? Which levels of protein structure would be affected?

I. Secondary Structure
II. Tertiary Structure
III. Quarternary Structure

(A) I Only
(B) III Only
(C) II and III Only
(D) I, II, and III
(D) I, II, and III

Chemical denaturants often disrupt the hydrogen bonding within a protein, thus affecting all levels of protein structure except for the primary structure.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What is typically thought of as the only method to denature the primary structure of a protein?
Using an enzyme is primarily thought of as the method to denature the primary structure of a protein and release individual amino acids.

You could also do this with EXTREME heat and pH.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
What happens to the conformational stability of an egg as it is being digested in your stomach?
Your digestive enzymes take the egg protein's linear polypeptide chain (primary structure still intact) and break peptide bonds in order to absorb amino acids into blood stream. We then can use the individual amino acids for protein synthesis.

Struggling with the one-letter abbreviations, three-letter abbreviations, structures, and the essential properties of Amino Acids? Learn how to conquer any Amino Acid MCAT question using Andrew's Amino Acid Mastery Course @ https://mcatselfprep.com/course/andrews-amino-acid-mastery-course/
Compare and contrast the two following alpha amino acid synthesis reactions: Gabriel Synthesis and Strecker Synthesis
Gabriel synthesis starts with N-pthalamidomalonic ester "Thad", which protects both the amine group and carboxylic acid. The alpha-carbon will be alkylated, hydrolyzed, and then heated for a decarboxylation.

Strecker Synthesis is much more simple and efficient, starts with ammonia, KCN, and an aldehyde/ketone. The aldehyde/ketone and ammonia will react to form an imine, which in acid with KCN will form a nitrile, and hydrolysis in acid will yield the alpha-amino-acid.

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