Thermophiles Lab Report

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There are many adaptations that can occur in thermophiles but some of the most common adaptations are an increased number of large hydrophilic residues, disulfide bonds, and ionic interactions. Adapting to have a large hydrophobic core is important when it comes to the folding and stability of the protein. Increasing disulfide bonds is important in preventing alteration to the protein structure. The increased disulfide bonds are also important in oligomerization. An example of this would be citrate synthetase fromprobaculum aerophium which showed that their use of disulfide bonds to create cyclized protein chains kept them form separating and allowing themselves to withstand the heat. Ionic interaction adaptations are seen in the desolvation …show more content…

They are usually made up of surfactants, which are surface active agents which reduce the surface tension of water by absorbing the common boundary between more than one liquid (3). The amphipathic character of detergents is evident in their structures, which consist of a polar (or charged) head group and a hydrophobic tail. Depending on the head of the detergent they can either be ionic, nonionic, and zwitterionic. This is dependent on the stereochemistry of the entire detergent. Detergent monomers self-associate to form structures called micelles. When the concentration exceeds the CMC, a detergent becomes capable of solubilizing hydrophobic and amphipathic molecules, such as lipids, into mixed micelles or micellar aggregates( ). In micelles, the amphiphilic lipid has a tail that forms a core that encapsulates an oil droplet or dirt particle and a head that maintains contact with the surrounding water environment. To work effectively, the chemical formation of micelles is not enough to remove oil or grease; mechanical energy (scrubbing or water flow) is often required …show more content…

The studied structure was the one of the E. coli glycerol uptake facilitator (GlpF), which is an aquaglyceroporin, i.e., the channel is also permeable to small linear sugar molecules such as glycerol. Nanosecond MD simulations of tetrameric GlpF in a hydrated patch of POPE lipid bilayer characterized the complete pathway of substrate conduction in the channel. Analysis of hydrogen bond interactions of the substrate with the interior of the channel also explained for the first time why these channels incorporate in their architecture two characteristic loops, including energetically unfavorable secondary structure elements, which are conserved in the whole aquaporin family (Jensen et al., Structure, 2001).

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