Sulfer hot springs are a common source of archaebacteria, the third domain of li

Question

Sulfer hot springs are a common source of archaebacteria, the third domain of life that biohemically may to be more similar to eukaryotes than bacteria. You have just read research indicating that archaebacteria may be a rich source of a novel family of proteins, the Querall family. These proteins bind to selenium and activate other proteins through an unusual sulfhydryl modification of amines within the cell to repair telomeres, restore replicative ability, and as a result, reverse the aging process. Though they bind selenium, they seem to have a basic pI, in the range of 8.7-9.5. They also tend to be in the size range of the most common archae proteins, ranging from 10 kDa to 90 kDa. Eager to begin your study, you've already set up your own aritificial hot spring and have a thriving culture of archaebacteria to sample. However, you now need to isolate the proteins. a. Describe a method for isolating these proteins. Focus on the overall strategies and steps rather than specific buffers and lysis techniques, but be sure to be specific with your rationale for each technique.

Explanation / Answer

Protein purification methods

Chromatography methods make the most of the physical properties involving sometimes the particular target protein or the particular other elements in the particular solution. In gas or liquid chromatography methods, the protein and their surrounding elements are typically dissolved in a mixture and then handed by having a non moving stage in advance of analysis. Centrifugation, purification, sonication and other fractionation techniques can often separate and take the particular mobile or portable areas that will surround and support the target protein, similar to mobile or portable membranes and DNA. For the duration of precipitation techniques, ammonium sulfate is usually put into solution and protein samples are obtained and centered while they precipitate. Using this method can often be utilized for bulk protein extraction. Gel electrophoresis techniques can often identify denatured or non-natured necessary protein by passing samples through an electronically charged gel matrix. The matrix typically sets apart the protein molecules by pH or molecular weight.

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