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HomeHomework HelpbiologyProtein Folding and Chaperones

Protein Folding and Chaperones

Protein folding refers to the process by which a polypeptide chain acquires its functional three-dimensional structure, which is essential for its biological activity. Chaperones are specialized proteins that assist in the proper folding of other proteins, preventing misfolding and aggregation during the folding process.

intermediate
3 hours
Biology
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Overview

Protein folding is a critical biological process that determines the functional shape of proteins. Proper folding is essential for protein activity, and chaperones play a vital role in assisting this process. Misfolded proteins can lead to serious diseases, highlighting the importance of understandi...

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Key Terms

Amino Acid
Building blocks of proteins.

Example: There are 20 different amino acids in proteins.

Peptide Bond
The bond formed between amino acids.

Example: Peptide bonds link amino acids in a protein chain.

Native State
The functional three-dimensional structure of a protein.

Example: Proteins must reach their native state to function properly.

Chaperone
Proteins that assist in the folding of other proteins.

Example: Heat shock proteins are a type of chaperone.

Misfolding
Incorrect folding of proteins, leading to dysfunction.

Example: Misfolding can cause diseases like Alzheimer's.

Prion
Infectious proteins that can cause misfolding.

Example: Prions are responsible for mad cow disease.

Related Topics

Protein Structure
Study of how proteins are built and organized.
intermediate
Enzyme Function
Understanding how proteins act as catalysts in biological reactions.
intermediate
Genetic Mutations
Exploring how changes in DNA can affect protein folding and function.
advanced

Key Concepts

Protein StructureFolding MechanismChaperone FunctionMisfolding Diseases