Biochemistry - Proteins and Structure Levels

Proteins change their shape by binding to other macromolecules, small molecules, or atoms, or by altering their environment.

True (A)

The fully active confirmation of a protein is called the native confirmation. It is the conformation where the protein functions optimally.

<p>True (A)</p> Signup and view all the answers

<p>The levels of protein structure are primary, secondary, tertiary, and quaternary.</p> Signup and view all the answers

<p>The primary structure is the foundation upon which the higher levels of structure are built.</p> Signup and view all the answers

<p>The primary structure of a protein determines its final shape.</p> Signup and view all the answers

<p>The stages for building a protein are making the base and folding. To make the base, we have types of amino acids and a sequence of amino acids.</p> Signup and view all the answers

<p>The primary structure involves covalent bonds, specifically peptide bonds.</p> Signup and view all the answers

<p>The secondary structure involves hydrogen bonds formed between nitrogen and oxygen atoms in the backbone.</p> Signup and view all the answers

<p>Ionic bonds (A), Hydrogen bonds (B), Disulfide bonds (D), Van der Waals interactions (E)</p> Signup and view all the answers

<p>These terms refer to the same thing - a single, independent polypeptide chain within a protein structure.</p> Signup and view all the answers

<p>We can tell by identifying the presence of a single N-terminal and a single C-terminal amino acid sequence. If there are more than one N-terminal and C-terminal, then it must contain multiple polypeptide chains.</p> Signup and view all the answers

<p>The quaternary structure is the association of multiple polypeptide chains that are linked together by various types of bonds. These proteins are known as multimeric proteins.</p> Signup and view all the answers

<p>Hemoglobin is a protein that delivers oxygen to body tissues.</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>True (A)</p> Signup and view all the answers

<p>True (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>Sickle-cell anemia is caused by a change in the 6th amino acid position of the Beta globin chain, replacing glutamic acid with valine.</p> Signup and view all the answers

<p>Glutamic acid is negatively charged and causes repulsion between hemoglobin molecules. When replaced with valine, which is hydrophobic, the hemoglobin molecules clump together, forming sickle shapes that impede blood flow and oxygen transport.</p> Signup and view all the answers

A protein's ability to change shape by binding to other molecules or altering its environment.

A specific shape of a protein that is fully active and functional.

The linear sequence of amino acids in a protein, held together by peptide bonds.

Localized arrangements of amino acids within a polypeptide chain due to hydrogen bonding, resulting in alpha-helices or beta-sheets.

The overall 3D shape of a protein formed by interactions between amino acids that are further apart in the sequence.

The arrangement of multiple polypeptide chains (subunits) in a protein, held together by various bonds.

A protein composed of more than one polypeptide chain.

The bond that holds amino acids together in a polypeptide chain.

Interactions that stabilize the tertiary structure of proteins, involving the attraction of oppositely charged groups.

Interactions that stabilize the tertiary structure of proteins, involving weak attractions between nonpolar side chains.

Interactions that stabilize the tertiary structure of proteins, involving temporary fluctuations in electron distribution, leading to weak attractions.

A covalent bond that can stabilize the tertiary structure of proteins, formed between two cysteine amino acids.

The end of a polypeptide chain that has a free amino group.

The end of a polypeptide chain that has a free carboxyl group.

The process of determining the sequence of amino acids in a protein.

The oxygen-carrying protein found in red blood cells that delivers oxygen to tissues.

The oxygen-carrying protein found in muscle cells, responsible for storing oxygen.

A genetic disorder caused by a single amino acid substitution in the beta chain of hemoglobin, leading to sickle-shaped red blood cells.

The change in the shape of a protein, which often leads to changes in its function.

The ability of proteins to change their conformation and function in response to changes in their environment.

The level of protein structure that describes the interactions between individual polypeptide chains in a multimeric protein.

A monomeric protein contains only one polypeptide chain.

The specific arrangement of amino acids that determines the function of a protein.

The change in the amino acid sequence of a protein, which can have consequences for its structure and function.

The process by which a protein achieves its correct 3D shape.

The study of the structure, function, and interactions of proteins.

The set of all proteins produced by an organism or cell.

The process of separating and identifying proteins based on their size, charge, or other properties.

The technique used to determine the 3D structure of proteins.