Use of Synthetic Peptides for the Study of Membrane Protein Structure

Living cells maintain tenfold or greater concentration gradients of Na +, K+, and Ca2+ across an ion-impermeant hydrocarbon layer approximately 30 Å thick in their lipid bilayer membranes

J. D. Lear

2013

Scholarcy highlights

  • Living cells maintain tenfold or greater concentration gradients of Na +, K+, and Ca2+ across an ion-impermeant hydrocarbon layer approximately 30 Å thick in their lipid bilayer membranes
  • Decades of study of nervous system and muscle physiology have since identified hundreds of functionally distinct ion channels
  • The apparent correlation of sequence features with channel functional type has prompted much curiosity and speculation concerning the three-dimensional structure and mechanisms of functioning of ion channel proteins
  • Given our current level of understanding of protein folding, such proteins are far too large and complicated for molecular modeling to provide a satisfactory level of structural detail
  • Comparative studies of natural sequence variations within channel families, functional analysis of site-directed mutations, and studies of synthetic peptides with sequences based on specific channel proteins are all being used

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