Protein Folding
Nature’s Origami: Protein Folding Is 'Hit And Miss' Process
Anyway, as proteins are released from the ribosomal machinery, the amino acid string can fold into various shapes, some causing disease even. So it is is not a case of making the amino acid string and the protein will magically self-organize into the right 3D-configuration. No, several other proteins (e.g. heat shock proteins - HSPs) guide amino acid strings into their correct configuration. It often happens that these HSPs become deficient, and this results in incorrectly folding proteins and disease.
From the article:
Video of protein folding.
To give an example, consider the following:
Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.
So even if proteins misfold, other quality control measures are at play to refold and prevent misfolding. When these mechanisms fail, cell death often follows.
Cells have their very own built-in natural selection system.
Nature’s Origami: Protein Folding Is 'Hit And Miss' Process
Intended purpose? Mmm, this guy should really beware of materialists, this might be mistaken for religious propaganda.ScienceDaily (Mar. 11, 2009) — Sometimes known as “nature’s origami”, the way that proteins fold is vital to ensuring they function correctly. But researchers at the University of Leeds have discovered this is a ‘hit and miss’ process, with proteins potentially folding wrongly many times before they form the correct structure for their intended purpose.
Anyway, as proteins are released from the ribosomal machinery, the amino acid string can fold into various shapes, some causing disease even. So it is is not a case of making the amino acid string and the protein will magically self-organize into the right 3D-configuration. No, several other proteins (e.g. heat shock proteins - HSPs) guide amino acid strings into their correct configuration. It often happens that these HSPs become deficient, and this results in incorrectly folding proteins and disease.
From the article:
The body’s proteins carry out numerous functions and play a crucial role in the growth, repair and workings of cells. Sheena Radford, Professor of Structural Molecular Biology at the University of Leeds, says: “There’s a fine balance between a protein folding into the correct shape so that it can carry out its job efficiently and it folding incorrectly, which can lead to disease. Just one wrong step can tip that balance.”
Proteins are made of amino acids arranged in a linear chain and the sequence of these amino acids is determined by the gene producing them. How these chains of amino acids are preprogrammed to fold into their correct protein structure is one of the mysteries of life.
The culmination of many years’ work, the collaborative study looked at the Im7 protein, a simple protein which is present in bacteria and has a crucial role to play in ensuring that bacteria do not kill themselves with the toxins they produce.
“Im7 is like an anti-suicide agent,” says Professor Radford. “We studied it partly because of its simplicity and partly because of the known evolutionary pressure on the protein to fold correctly to enable the bacteria to survive.”
The study has revealed that these proteins misfold en route to their intended structure, and importantly, has shown the forces at work during the folding process. While the chain of amino acids determines which shape a protein needs to take, the researchers discovered that it was the very amino acids central to the protein’s function that were causing the misfolding.
“This breakthrough could have huge implications for understanding the evolution of today’s protein sequences and in determining the balance between heath and disease,” says Professor Radford. “It’s fundamental science, but significant for our understanding of the mechanisms at work in the human body.”
This research was funded by the Biotechnology and Biological Sciences Research Council, with further support from various organisations including EMBO, the Leverhulme Trust, the Royal Society, and the Medical Research Council. The study was carried out in collaboration with scientists at the University of Cambridge, and the University of Leeds’ School of Physics and Astronomy.
Video of protein folding.
To give an example, consider the following:
Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.
In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this network are two protein families, the AAA+ and the Hsp70 family. The major Hsp70 chaperone. DnaK, efficiently prevents protein aggregation and supports the refolding of damaged proteins. In a special case, DnaK, together with the assistance of the AAA+ protein ClpB, can also refold aggregated proteins. Other Hsp70 systems have more specialized functions in the cell, for instance HscA appears to be involved in the assembly of Fe/S proteins. In contrast to ClpB, many AAA+ proteins associate with a peptidase to form proteolytic machines which remove irreversibly damaged proteins from the cellular pool. The AAA+ component of these proteolytic machines drives protein degradation. They are required not only for recognition of the substrate but also for substrate unfolding and translocation into the proteolytic chamber. In many cases, specific adaptor proteins modify the substrate binding properties of AAA+ proteins. While chaperones and proteases do not appear to directly cooperate with each other, both systems appear to be necessary for proper functioning of the cell and can, at least in part, substitute for one another.
So even if proteins misfold, other quality control measures are at play to refold and prevent misfolding. When these mechanisms fail, cell death often follows.
Cells have their very own built-in natural selection system.
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