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Chaperones - Discovery Of Chaperones, Recognizing And Correcting Mistakes, Two Common Chaperone Systems: Hsp70 And Hsp60

chains folded misfolded proteins

Molecular chaperones are proteins and protein complexes that bind to misfolded or unfolded polypeptide chains and affect the subsequent folding processes of these chains. All proteins are created at the ribosome as straight chains of amino acids, but must be folded into a precise, three-dimensional shape (conformation) in order to perform their specific functions. The misfolded or unfolded polypeptide chains to which chaperones bind are said to be "non-native," meaning that they are not folded into their functional conformation. Chaperones are found in all types of cells and cellular compartments, and have a wide range of binding specificities and functional roles.

Chromosomal Aberrations - Advances In Chromosomal Analysis, Chromosomal Aberrations, Aneuploidy, Disorders Associated With Aneuploidy, Abnormalities Of Chromosomal Structure - Unbalanced Chromosome Rearrangements [next] [back] Centromere

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