Chapter 4:Amino Acids Quiz
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The net charge of the zwitterion form of Gly is . A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

K

When a peptide bond is formed, an reacts with a carboxylate group. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

E

At a pH above its pK , the phenol group of tyrosine is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

C

In the tripeptide Lys─Pro─Ile, there are charged groups at pH 7. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>D</p> Signup and view all the answers

At a pH below its pK , the -amino group of lysine is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>L</p> Signup and view all the answers

At a pH below its pK , the -carboxylate group of Asp is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>B</p> Signup and view all the answers

In the peptide Trp─Ser─Val, valine is at the
A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>G</p> Signup and view all the answers

In the tripeptide Trp─Val─Phe, the N-terminal residue is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>N</p> Signup and view all the answers

In the tripeptide Lys─Pro─Ile, the C-terminal residue is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>M</p> Signup and view all the answers

Biological systems usually produce a single enantiomer, whereas chemical synthesis produces a A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>I</p> Signup and view all the answers

GABA is a neurotransmitter derived from A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>A</p> Signup and view all the answers

Glutathione is a tripeptide containing a central. residue. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus

<p>J</p> Signup and view all the answers

In the early 1930’s William Rose fed laboratory rats a mixture of all 19 amino acids known to be present in proteins. He observed that his rats lost weight. This observation led to the discovery of _ as the 20th amino acid found in proteins.

<p>Thr</p> Signup and view all the answers

What percentage of the 20 amino acids is considered to be nutritionally essential to lab animals?

<p>50%</p> Signup and view all the answers

About half of the 20 amino acids are called essential because

<p>our bodies cannot synthesize them and therefore they need to be present in our diet.</p> Signup and view all the answers

Which amino acid does not have a primary -amino group?

<p>proline</p> Signup and view all the answers

Which of the following statements is true?

<p>Purines and pyrimidines can be derived from amino acids.</p> Signup and view all the answers

Which of the following amino acids is the least abundant in proteins?

<p>W</p> Signup and view all the answers

Zwitterions are

<p>ions that bear both negatively and positively charged groups.</p> Signup and view all the answers

The formation of a dipeptide from two amino acids involves

<p>loss of water.</p> Signup and view all the answers

Which of the following amino acids has a charged polar side chain at pH 7.0?

<p>Glu</p> Signup and view all the answers

Which of the following tripeptides carries a net positive charge at pH 7.0?

<p>Leu─Lys─Gly</p> Signup and view all the answers

Which of the following amino acids has a sulfur atom in its side chain?

<p>Met</p> Signup and view all the answers

Which of the following amino acids does not have an ionizable side chain

<p>Asn</p> Signup and view all the answers

Which of the following amino acids has an uncharged polar side chain at pH 7.0?

<p>Thr</p> Signup and view all the answers

The ionization of amino acids depends on the pH and the pK s of the ionizable groups. The pK and pK for the amino acid shown above are 2.1 and 8.8, respectively. At what pH is the amino acid ionized predominantly as shown?

<p>1.0</p> Signup and view all the answers

The pK1 , pK 2, and pKr for the amino acid arginine are 1.8, 9.0, and 12.5, respectively.

At pH 7.0 arginine would be charged predominantly as follows:

<p>-carboxylate −1, -amino +1, guanidino +1, net charge +1</p> Signup and view all the answers

The pK1 , pK 2, and pKr for the amino acid aspartic acid are 2.0, 9.9, and 3.9, respectively.

At pH 7.0, aspartic acid would be charged predominantly as follows:

<p>-carboxylate −1, -amino +1, -carboxylate −1, net charge −1</p> Signup and view all the answers

The pK 1, pK2 , and pK rfor the amino acid glutamate are 2.1, 9.5, and 4.1, respectively.

At pH 11.0, glutamate would be charged predominantly as follows:

<p>-carboxylate −1, -amino 0, -carboxylate −1, net charge −2</p> Signup and view all the answers

While proteins are usually composed of linear chains of amino acids, branched chains of amino acids and internally cross-linked chains can be found in certain proteins. Polypeptide chains are most commonly linked to each other through

<p>disulfide bonds.</p> Signup and view all the answers

The disulfide bond between two cysteine molecules

<p>is a covalent bond formed by oxidation.</p> Signup and view all the answers

The tripeptide glycylarginylglutamate contains four ionizable groups with pK s of 2.1, a 4.1 9.8, and 12.5. Calculate the pI for this molecule.

<p>7.0</p> Signup and view all the answers

The tripeptide alanyllysylaspartate contains four ionizable groups with pK s of 2.0, 3.9, a 9.9, and 10.5. Calculate the pI for this molecule.

<p>none of the above</p> Signup and view all the answers

The isoelectronic point of an amino acid is the point where

<p>the amino acid carries no net electrical charge.</p> Signup and view all the answers

The side-chains of amino acids have

<p>different pK s in peptides as compared to the free amino acids</p> Signup and view all the answers

The peptide AYDG has an N-terminal residue.

<p>alanine</p> Signup and view all the answers

Which of the following tripeptides would be expected to be the most hydrophobic?

<p>GYA</p> Signup and view all the answers

What is the three-letter abbreviation for the peptide valylarginylisoleucine?

<p>Val─Arg─Ile</p> Signup and view all the answers

Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because

<p>they have a configuration of groups around the C that can be related to the configuration of groups around the asymmetric carbon in L-glyceraldehyde.</p> Signup and view all the answers

Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because

<p>None of the above</p> Signup and view all the answers

Which of the amino acids represented below has two chiral centers?

<p>Ile</p> Signup and view all the answers

All the standard amino acids except are optically active.

<p>Fly</p> Signup and view all the answers

The character of most standard amino acids causes solutions of amino acids to rotate the plane of polarized light.

<p>Chrial</p> Signup and view all the answers

All amino acids derived from proteins have the same stereochemical conformation as.

<p>L-glyceraldehyde.</p> Signup and view all the answers

Typically, modified amino acids, those with side chain modifications that are present in proteins

<p>are formed by modification of standard side chain residues after the protein is synthesized.</p> Signup and view all the answers

An amide bond between a side-chain carboxylate and an -amino group is also called a(n)

<p>isopeptide bond.</p> Signup and view all the answers

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