Protein folding

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Protein folding

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from a random coil.

Pronunciation

Protein folding: /ˈproʊtiːn ˈfoʊldɪŋ/

Etymology

The term "protein folding" is derived from the words "protein", which comes from the Greek word "proteios" meaning "primary" or "in the lead", and "folding", which refers to the way in which the protein's structure is folded into its final shape.

Process

The process of protein folding involves the amino acid sequence or the primary structure of the protein. The sequence of amino acids determines the protein's structure and specific function. The process of folding often begins co-translationally, so that the N-terminus of the protein begins to fold while the C-terminal portion of the protein is still being synthesized by the ribosome.

Misfolding and diseases

Misfolded proteins can create a variety of health problems, known as protein misfolding diseases, or conformational diseases. These include Alzheimer's disease, Parkinson's disease, and Huntington's disease.

Related terms

  • Chaperone (protein): A type of protein that assists in the folding of other proteins.
  • Denaturation (biochemistry): The process by which proteins lose their structure.
  • Proteopathy: A type of disease caused by proteins that have become structurally abnormal, and typically forming aggregates.
  • Proteostasis: The concept that there are many processes in cells that control the concentration, folding, interactions and localization of proteins.

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