Search results
Results from the WOW.Com Content Network
Numerous protein structures are the result of rational design and do not exist in nature. Proteins can be designed from scratch (de novo design) or by making calculated variations on a known protein structure and its sequence (known as protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to ...
The duration of the folding process varies dramatically depending on the protein of interest. When studied outside the cell, the slowest folding proteins require many minutes or hours to fold, primarily due to proline isomerization, and must pass through a number of intermediate states, like checkpoints, before the process is complete. [7]
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
Such proteins violate Anfinsen's dogma, [14] requiring protein dynamics to fold correctly. Other types of chaperones are involved in transport across membranes, for example membranes of the mitochondria and endoplasmic reticulum (ER) in eukaryotes.
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
Protein folds describe similar spatial arrangements of regular secondary structures in the proteins. They are helpful for structural classification of proteins . Subcategories
Most proteins fold into unique 3D structures. The shape into which a protein naturally folds is known as its native conformation. [36]: 36 Although many proteins can fold unassisted, simply through the chemical properties of their amino acids, others require the aid of molecular chaperones to fold into their native states.
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. [5] It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES.