Protein Structure and Function

Active site of a protein that changes shape upon binding with a molecule, influencing its function.

Proteins that help other proteins fold correctly.

A protein that binds to DNA and regulates gene expression. Often mutated in cancer.

The process by which proteins are synthesized only when and where they are needed.

The process by which proteins are transported to their specific location within the cell.

A modification to a protein after it has been synthesized, often altering its function.

The process by which proteins are broken down into amino acids.

A protein that has folded incorrectly, potentially leading to aggregation and disease.

A group of misfolded proteins that clump together, potentially causing disease.

The process by which a protein is transported from the cytosol into the endoplasmic reticulum.

The linear sequence of amino acids in a polypeptide chain. It is determined by the genetic code and dictates the protein's overall structure and function.

A covalent bond formed by the removal of water between the carboxyl group of one amino acid and the amino group of the next. It links amino acids together in a polypeptide chain.

A type of secondary protein structure where the polypeptide chain twists into a right-handed helix. It is stabilized by hydrogen bonds between the peptide backbone.

A type of secondary protein structure where the polypeptide chain folds into a sheet-like structure. It is stabilized by hydrogen bonds between the peptide backbones of adjacent strands.

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 three-dimensional shape of a protein, determined by the interactions between its amino acid side chains. It is crucial for protein function.

The arrangement of multiple polypeptide chains (subunits) in a protein complex. It involves interactions between the subunits, such as hydrophobic interactions, ionic bonds, and hydrogen bonds.

A type of secondary structure in proteins where polypeptide chains align side-by-side, forming hydrogen bonds between the N-H and C=O groups. It can be either parallel or anti-parallel, depending on the direction of the strands.

Beta sheets can stack together in long rows. Beta barrels are an example of a structure formed through the stacking of Beta sheets.

The overall 3D structure of a protein, often formed by folding into the lowest free energy state (G)

Weak interactions that contribute to the stability of a protein's tertiary structure.

Interactions between polar groups in a protein, involving the sharing of a hydrogen atom between two electronegative atoms like oxygen or nitrogen.

Interactions between charged groups in a protein, based on attraction between opposite charges.

Strong covalent bonds formed between sulfur atoms in cysteine residues, contributing to the stability of the protein's tertiary structure.

The tendency for hydrophobic amino acid side chains to cluster together in the interior of a globular protein, away from the surrounding water molecules.

A complex formed by two or more polypeptide chains bound together. The chains are called subunits, and they bind at specific points called binding sites.

A stable, independently folded segment of a protein that often carries out a specific function. Proteins can have one or more domains.

Proteins with elongated structures, typically made of strands of polypeptide chains coiled around each other. Examples include collagen and elastin.

Proteins with spherical shapes, often with hydrophobic regions facing inwards. Many enzymes are globular proteins.

The ability of a protein to change its shape, often in response to changes in the environment or binding of ligands. This can be important for protein function.