Chemical Probes for the Geometry of Membrane Proteins

  • Frederic M. Richards
  • James V. Staros
  • Kuan Wang
  • H. Heitzmann


The position of the protein components of biological membranes both perpendicular to and in the plane of the permeability barrier has been the subject of much recent interest. The “sidedness” of the identifiable peptide chains has been examined with low-molecular-weight reagents similar to those used in modification studies on soluble proteins, and with such macromolecular reagents as enzymes or binding proteins. With the former category, use is made of nucleophilic groups on the exposed side chains of the proteins as the required reaction sites (BERG, 1969; BRETSCHER, 1971a, b, c; STECK, 1972; WHITELEY, BERG, 1974), while enzymes need exposed peptide bonds for proteolysis (BENDER et al., 1971; STECK et al., 1971; STECK, 1972; TRIPLETT, CARRAWAY, 1972) or aromatic side chains for iodination reactions (PHILLIPS, MORRISON, 1971a, b; 1973); lectins act as specific sugar binding reagents (e.g., NICOLSON, SINGER, 1974). These studies have recently been reviewed by WALLACH (1972), BRETSCHER (1973), ZWALL et al. (1973), STECK (1974), and SINGER (1974).


Sugar Aldehyde Fractionation Oligomer Disulfide 


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Copyright information

© Springer-Verlag Berlin Heidelberg 1975

Authors and Affiliations

  • Frederic M. Richards
    • 1
  • James V. Staros
    • 1
  • Kuan Wang
    • 1
  • H. Heitzmann
    • 1
  1. 1.Department of Molecular Biophysics and BiochemistryYale UniversityNew HavenUSA

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