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Nitchakan Chaiprukmalakan

Proteins and quantum transition: Instant shape-shifting - 0 views

  • The genetic code in DNA provides the template to manufacture protein into all the cells of an organism.
  • Proteins are made by stringing together amino acids. For general purposes there are twenty amino acids in protein and they can be put together in endless combinations, some in short chains (yeast averages 466 amino acids), some long chains (titins have nearly 27,000 amino acids) and everything in-between. The pattern of amino acids determines much of the functionality of the protein.
  • Proteins are three-dimensional puzzle pieces. They are generally very complicated in shape. Even a small protein of only 100 amino acids can theoretically have 10^100 (ten to the hundredth power) different configurations.
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  • most protein reconfigurations occur in nanoseconds
  • In research on proteins, it was assumed (given their chemical composition) proteins would uniformly fold as they cool down and unfold as they heat up. (Think of a balloon expanding and shrinking with the temperature of the air inside.) The experiments didn’t bear this out; the rate of folding or unfolding according to temperature change was unequal (asymmetric) and uneven (nonlinear).
  • In recent biochemistry a great deal of work is done with ‘tagging’ or ‘marking’ molecules with fluorescent and phosphorescent materials. It’s well known that fluorescence and phosphorescence are phenomena closely related to protein folding and they can only be understood in terms of quantum transition between molecules.
  • With a quantum transition, the protein could change configuration by ‘jumping’ – skipping all the transition steps – to the final configuration. They call this quantum folding and they developed a mathematical model that shows how the folding, which is virtually instantaneous, would react to change in temperature.
  • Their quantum transition model matched the folding curves for 15 different proteins and also provides an explanation for the different rates of folding and unfolding among these proteins.
  • Luo and Lu’s paper is short, a mere 16 pdf pages, and the model is unpretentious mathematically. (Luo has several other related papers on arXiv.) It comes from unknown researchers in an unknown corner of the academic world, and it’s published on the open-source arXiv system. The lack of pedigree means that it will take more time than usual for scientists around the world to learn of it, examine it, and possibly test it.
    • Nitchakan Chaiprukmalakan
       
      This is not accepted as a true fact yet and has to be proven.
Rafael Chen

Biotechdaily - First Microbes Found to Break Down PCBs - 0 views

  • PCBs can buildup in fish and marine mammals, reaching thousands of times higher levels than found in the water they live in
  • using a rapid, DNA screening method, researchers have discovered a bacterium capable of degrading PCBs
  • this will lead to the complete dechlorination of persistant molecules
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  • important for bioremediation efforts and for developing molecular probes to monitor PCB degrading
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    Using DNA screening method, researchers have discovered a bacterium capable of degrading PCBs
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