Biochem Sept. 8th

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Vocabulary flashcards covering energy changes (ΔG), the central dogma, and fundamental concepts about amino acids, peptide bonds, and protein structure.

Last updated 6:28 PM on 10/30/25
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18 Terms

1
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What way is a sequence of amino acids read?

  • The sequence of amino acids in a protein is read from the N-terminus to the C-terminus.

  • Usually methionine (Met) initiates the chain 

2
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What determines the proteins chemical properties and folding behaviour?

The R group side chain of amino acids

3
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What are amino acids made of?

Amino acids are made of an amino group(NH3+), a carboxyl group (COO-), and an R group side chain, all attached to a central carbon atom.

4
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What do mutations or DNA damage do?

Mutations and DNA damage can alter the sequence of amino acids in proteins, changing protein structure and function, which underlies many diseases.

5
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What is a peptide bond?

A peptide bond is a covalent bond that links amino acids together, formed through a dehydration (removal of water) reaction between the amino group (NH3+) of one amino acid and the carboxyl group (COO-) of another.

<p>A peptide bond is a covalent bond that links amino acids together, formed through a dehydration (removal of water) reaction between the amino group (NH3+) of one amino acid and the carboxyl group (COO-) of another. </p>
6
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What are the amino acids that have hydrophobic R groups

Alanine, Valine, Proline, Leucine, Isoleucine, Phenylalanine, Tryptophan, and Methionine

7
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What are the amino acids with polar R groups?

Serine, Threonine, Cysteine, Asparagine, Glutamine, Tyrosine, and Histidine. These amino acids can form hydrogen bonds and interact with water, making them hydrophilic.

8
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What are the amino acids with charged R groups?

Lysine, Arginine, Aspartate, and Glutamate. These amino acids have side chains that can gain or lose protons, thus acquiring a charge and affecting their behavior in a protein's structure and function.

9
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What amino acids have ionizable groups?

lysine, arginine, glutamate, aspartate, cystine, histidine and tyrosine. Obvi all do with the C-terminus and N-terminus groups being ionizable)

10
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What is the Ka?

The acid dissociation constant, a measure of the strength of an acid in solution.

11
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What is the pKa?

The negative logarithm of the acid dissociation constant (Ka), which indicates the pH at which an acid is half dissociated.

12
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Lower the pKa ..

The stronger the acid

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What does it mean when the pH of a solution is equal to the pKa of that acid (pH = pKa) ?

Half of the molecules are in the protonated form (HA) and half are deprotonated (A-)

(Charge is either 0.5 or -0.5)

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pH = pKa + 1

~91% in A⁻

~9% in HA

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pH = pKa - 1

~9% in A⁻
~91% in HA

  • (Ex. Tyrosine has a pKa of 10 and the pH is 9, what’s the average net charge? Answer = -0.1 because 0.09 is basically 0.1)

    • -0.1 because 10% of it is in the deprotonated form and 90% is the neutral form -0.1 + 0 = -0.1

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pH = pKa + 2

~99% in A⁻

~1% in HA

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pH = pKa - 2

~1% in A⁻

~99% in HA

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<p>Net charge of amino acids</p><p>Ex. Asp at pH 7</p>

Net charge of amino acids

Ex. Asp at pH 7

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