Dobramento de proteínas: entendendo a dança dos chaperones

sexta-feira, março 09, 2012

Protein Folding: Understanding the Dance of the Chaperones

ScienceDaily (Mar. 8, 2012) — Proteins are the molecular building blocks and machinery of cells and involved in practically all biological processes. To fulfil their tasks, they need to be folded into a complicated three-dimensional structure. Scientists from the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, have now analysed one of the key players of this folding process: the molecular chaperone DnaK. "The understanding of these mechanisms is of great interest in the light of the many diseases in which folding goes awry, such as Alzheimer's or Parkinson's," says Ulrich Hartl, MPIB director.


The chaperone DnaK binds to new proteins and mediates their folding. Proteins it cannot fold, DnaK transports to GroEL, a highly specialised folding machine. (Credit: MPI of Biochemistry)



The work of the researchers has now been published in Cell Reports.


Proteins are responsible for almost all biological functions. The cells of the human body continuously synthesize thousands of different proteins in the form of amino acid chains. In order to be biologically useful, these chains must fold into a complex three-dimensional pattern. When this difficult process goes wrong, it can lead to useless or even dangerous protein clumps. All cells, from bacteria to human, have therefore developed a network of molecular chaperones, proteins themselves, which help other proteins to fold properly.
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