0
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      How proteins adapt to a membrane–water interface

      ,
      Trends in Biochemical Sciences
      Elsevier BV

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Membrane proteins present a hydrophobic surface to the surrounding lipid, whereas portions protruding into the aqueous milieu expose a polar surface. But how have proteins evolved to deal with the complex environment at the membrane-water interface? Some insights have been provided by high-resolution structures of membrane proteins, and recent studies of the role of individual amino acids in mediating protein-lipid contacts have shed further light on this issue. It now appears clear that the polar-aromatic residues Trp and Tyr have a specific affinity for a region near the lipid carbonyls, whereas positively charged residues extend into the lipid phosphate region.

          Related collections

          Author and article information

          Journal
          Trends in Biochemical Sciences
          Trends in Biochemical Sciences
          Elsevier BV
          09680004
          September 2000
          September 2000
          : 25
          : 9
          : 429-434
          Article
          10.1016/S0968-0004(00)01626-1
          10973056
          15c65f4e-6efe-4f3f-88f8-2d4c1505fcd2
          © 2000

          https://www.elsevier.com/tdm/userlicense/1.0/

          History

          Comments

          Comment on this article