2. Cell Chemistry & Cell Components

Proteins

2. Cell Chemistry & Cell Components

Proteins

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5 Protein-Related Terms

Denatured Proteins & Chaperones

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01:14

Short Video: Cotranslational Transport

BioFlix: Protein Modifications

Animation: Protein Structure

Animation: Protein Functions

Post-translational Modifications and Chaperone Proteins

Post Translation Modification

Post Translational Modifications

Post Translational Modifications Of Proteins

Post-Translational Modification of Proteins

PremedHQ Science Academy

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05:21

Protein Structure and Folding

Major Elements in Biological Molecules: Proteins

Biomolecules: The Proteins

Structure and function of Biological Macromolecules

Proteins | Biological Molecules Simplified #2

#1 A Level Biology - Biological Molecules

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Multiple Choice

The primary building blocks (monomers) of proteins are:

Which two functional groups are always found in amino acids?

What term is used for an amino acid chain that has greater than 50 covalently linked amino acids?

The specific amino acid sequence in a protein is its:

Which of the following is true of protein structure?

What is the role of a chaperone protein?

The overall three-dimensional shape of a single polypeptide is called its __________.

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Multiple Choice

When a protein is denatured, why does it lose its functionality?

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Multiple Choice

Which of the following lists ranks these molecules in the correct order by size from smallest to largest?

Which of the following represents a specific description of a polypeptide?

Enzyme molecules require a specific shape to perform their catalytic function. Which of the following might alter the shape of an enzymatic protein?

The peptide bond is __________.

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Multiple Choice

The α helix and β pleated sheet represent which level of protein structure?

Protein molecules are polymers (chains) of __________.

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Multiple Choice

What do Alzheimer's, Parkinson's, and mad cow disease have in common?

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Multiple Choice

The "primary structure" of a protein refers to __________.

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Textbook Question

What type of bond is directly involved in the formation of an α-helix? a. peptide bonds between amino acid residues b. hydrogen bonds between amino acid residues c. van der Waals interactions between nonpolar residues d. disulfide bonds between cysteine residues

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Textbook Question

What type of information is used to direct different polypeptides to fold into different shapes?

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Textbook Question

The structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary level. b. secondary level. c. tertiary level. d. quaternary level.

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Textbook Question

If a cell were to use only 10 of the 20 possible amino acids, how much effect would you expect this to have on protein diversity? Calculate and compare the number of different sequences that can be generated by randomly assembling either 10 or 20 amino acids into peptides that are five residues long.

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Textbook Question

Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.

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Textbook Question

Different proteins are composed of different sequences of . a. sugars; b. lipids; c. fats; d. amino acids; e. carbohydrates

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Textbook Question

Why are proteins not considered to be a good candidate for the first living molecule? a. Their catalytic capability is not sufficient for most biological reactions. b. Their amino acid monomers were not likely present in the prebiotic soup. c. They cannot serve as a template for replication. d. They could not have polymerized from amino acid monomers under early Earth conditions.

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Textbook Question

Predict the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure.

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Textbook Question

Proteins may function as . a. genetic material; b. cholesterol molecules; c. fat reserves; d. enzymes; e. all of the above

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Textbook Question

Based on what you know of the peptide bonds that link together amino acid residues, why would proline's side chain reduce the flexibility of the backbone?

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Textbook Question

Which structural level of a protein would be least affected by a disruption in hydrogen bonding? a. primary structure b. secondary structure c. tertiary structure d. quaternary structure

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Textbook Question

Make a concept map (see BioSkills 12) that relates the four levels of protein structure and shows how they can contribute to the formation of hemoglobin. Your map should include the following boxed terms: Primary structure, Secondary structure, Tertiary structure, Quaternary structure, Amino acid sequence, R-groups, αα-helices, and ββ-pleated sheets.

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Textbook Question

Most proteins are soluble in the aqueous environment of a cell. Knowing that, where in the overall three-dimensional shape of a protein would you expect to find amino acids with hydrophobic R groups?

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Textbook Question

What are the two types of secondary structures found in polypeptides, and what maintains them? What stabilizes the tertiary structure of a polypeptide?

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Textbook Question

How can a cell make many different kinds of proteins out of only 20 amino acids? Of the myriad possibilities, how does the cell 'know' which proteins to make?

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Textbook Question

Mark the following statements as true or false. If a statement is false, correct it to make a true statement.

d. Proteins are composed of strings of fatty acids linked by glycosidic bonds.

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Textbook Question

An enzyme is a:

a. biological catalyst that increases the concentration of the products.

b. biological catalyst that increases the concentration of the reactants.

c. chemical that is used in a reaction, after which it can no longer be used by the cell.

d. biological catalyst that works by bringing its substrates closer to their transition states.

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Textbook Question

Why is it important for a protein to maintain its structure? What is it called when a protein loses its structure?

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2. Cell Chemistry & Cell Components

Proteins

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