• Title of article

    The well-tempered protein

  • Author/Authors

    Gabriel F. Berriz، نويسنده , , Gabriel F and Shakhnovich، نويسنده , , Eugene I، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 1999
  • Pages
    11
  • From page
    72
  • To page
    82
  • Abstract
    Globular proteins are the most functionally versatile class of molecules in the biosphere. They play leading roles in practically every aspect of cell physiology, including gene expression, developmental and metabolic regulation, transport, and catalysis. Essential to a proteinʹs function is its characteristic and geometrically well-defined three-dimensional shape, or native state. Proteins, however, are synthesized by the cell as biologically inactive linear chains; it is only upon folding to their native states that globular proteins come to life. The general principles underlying the behavior of proteins as amphiphilic heteropolymer molecules, as well as those unique properties of proteins as biopolymers that are evolutionarily selected for folding and function are important for understanding globular proteins. Recently, there have been many successes in recent studies of lattice and off-lattice coarse-grained models of proteins, as well as in the main current challenges facing the field. © 1999 Elsevier Science Ltd.
  • Journal title
    Current Opinion in Colloid and Interface Science
  • Serial Year
    1999
  • Journal title
    Current Opinion in Colloid and Interface Science
  • Record number

    2304706