![]() Unlike regular proteins, which unfold and lose their ability to function when subjected to environmental challenges such as detergents, urea, or heat, IUP may continue to function under such conditions, as they do not have to be folded into a particular configuration in order to carry out their function. These proteins have been variously called natively unfolded, natively disordered or Intrinsically Unstructured regions and Proteins (IUP). Recently, a class of proteins has been discovered that do not fold into any particular configuration – instead of folding into specific 3-D structures, they exist as dynamic ensembles in their native state. Most proteins function only when folded into a particular configuration. The tertiary structure is defined by how the chain folds into a three-dimensional configuration, while the quaternary structure is concerned with how different chains combine into multisubunit or oligomeric, protein (protein complexes). The primary structure is defined by the sequence of amino acids comprising each chain, while the secondary structure is defined by local, repetitive spatial arrangements, which falls into three basic categories: helix, strand, and coil. Proteins are composed of one or more chains of amino acids, and exhibit several levels of structure.
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