CAS BI 108 Chapter Notes - Chapter 3: Peptide Synthesis, Tryptophan, Threonine

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brownhare818

9 Feb 2017

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Document Summary

Unfortunately, (3) in the previous paragraph is a bit of a lie; tyrosine has an oxygen and tryptophan has a nitrogen. Proline looks like it has a nitrogen, but this is actually the backbone nitrogen and does not count. I will not try to trick you by asking whether tyrosine, tryptophan or proline are hydrophilic or hydrophobic. These 20 amino acids are incorporated into peptides by the ribosome during peptide synthesis, which is a process called translation. amino acids are often modi ed after translation. The most common modi cation is phosphorylation, which most often occurs on the oh group of serine, threonine or tyrosine. Proteins: primary structure, secondary structure, tertiary structure and. Primary structure for proteins refers to the amino acid sequence. Secondary structure refers to the shape adopted by the amino acid backbone, where two shapes are common: the -helix and the -strand, which are discussed at greater length below.

Related Questions

1) Which three amino acids are most the frequent targets of post-translational modification via phosphorylation?

A) cysteine, proline, serine

B) proline, serine, tyrosine

C) serine, threonine, tyrosine

D) arginine, aspartic acid, glutamic acid

2) In an alpha helix structure of a protein, the amino acid side groups are positioned...

A) in the hydrophobic interior of the helix (this is not the right answer, I put this answer choice already and it was wrong)

B) in the interior of the hydrophilic interior of the helix

C) outside of the helix

D) on both the outside and inside of the helix

E) None of the above. Amino acids in alpha helices do not have side groups.

orangedinosaur998

Protein Structure

a.Different function of proteins and examples:

b. Protein building blocks:

1. atomic composition of building block:

2. "parts" or "functional groups" of the building block:

c. Importance of side chain (R group):

d. Hydrophobic amino acids characteristics:

e. Hydrophilic amino acids characteristics:

f. Charged amino acids characteristics

Copy and complete the table below regarding the characteristics and which groups in the polypeptide interact together at each structural level of the protein.

	characteristics	groups interacting
Primary structure
Secondary structure
Tertiary structure
Quartenary structure

Value: 2

Choose the correct statement(s). You may choose more than one answer.

[mark all correct answers]
a. Proteins are the building blocks of amino acids.

b. Enzymes are a type of protein.

c. Quartenary structure consists of two or more polypeptide chains interacting.

d. Amino acids are made of carbon, hydrogen, nitrogen and phosphorus.

e. The primary structure of a protein is formed due to the interaction of side groups.

Value: 3

Put the following statements regarding the structural levels of a protein formation in the correct order.

Below is a sequence of events. Place them in the order they should occur, number 1 being the first item. Select the step number from the drop down next to each item.

Items to order:

1. Individual amino acids are bonded together via peptide bonds.

2. Two or more polypeptide chains interact via bonds.

3. Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

4. Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

Value:4

Put the following statements regarding the structural levels of a protein formation in the correct order

Individual amino acids are bonded together via peptide bonds.	1 2 3 4
Two or more polypeptide chains interact via bonds.	1 2 3 4
Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.	1 2 3 4
Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.	1 2 3 4