FirstGlance/Visualizing Conservation: Difference between revisions
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Tryptophans are known to orient at, and parallel to, the apolar-polar interface in transmembrane channels such as the potassium channel<ref name="koeppe2008">PMID: 18550546</ref><ref name="allen2013">PMID: 22989724</ref><ref name="walrant">[https://www.mdpi.com/2073-4352/11/9/1032/htm Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins], Sonia Khemaissa, Sandrine Sagan, | Tryptophans are known to orient at, and parallel to, the apolar-polar interface in transmembrane channels such as the potassium channel<ref name="koeppe2008">PMID: 18550546</ref><ref name="allen2013">PMID: 22989724</ref><ref name="walrant">[https://www.mdpi.com/2073-4352/11/9/1032/htm Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins], Sonia Khemaissa, Sandrine Sagan, | ||
and Astrid Walrant. ''Crystals'', 2021, '''11'''(9), 1032; [https://doi.org/10.3390/cryst11091032 doi.org/10.3390/cryst11091032].</ref>. Let's see which Trps are conserved in the potassium channel [[1bl8]]. | and Astrid Walrant. ''Crystals'', 2021, '''11'''(9), 1032; [https://doi.org/10.3390/cryst11091032 doi.org/10.3390/cryst11091032].</ref>. Let's see which Trps are conserved in the potassium channel [[1bl8]] (a [[Nobel_Prizes_for_3D_Molecular_Structure#2000-2009|Nobel Prize-winning structure]]!). | ||
:[https://www.bioinformatics.org/firstglance/fgij3.8beta3/fg.htm?mol=1bl8_consurf1640894833_pipe.pdb Display 1BL8 ConSurf Result in FirstGlance 3.8Beta3] | :[https://www.bioinformatics.org/firstglance/fgij3.8beta3/fg.htm?mol=1bl8_consurf1640894833_pipe.pdb Display 1BL8 ConSurf Result in FirstGlance 3.8Beta3] | ||