Characterization of a Transient intermediate in the Folding of Dihydrofolate Reductase

  • C. Robert Matthews
  • Edward P. Garvey
  • Jonathan Swank
Part of the Industry-University Cooperative Chemistry Program Symposia book series (IUCC)


The central dogma of molecular biology describes the flow of genetic information from DNA to RNA (transcription) and from RNA to protein (translation). Although the information is stored and expressed in a linear format, the final product spontaneously folds to a unique three dimensional structure which is required for function. The past three decades have seen tremendous advances in our understanding of the processes of transcription and translation, however, rather little is known about the details of how the amino sequence of a protein directs the rapid and efficient folding to the native conformation.


Tryptophan Residue Dihydrofolate Reductase Native Conformation Solvent Exposure Hydrophobic Cluster 
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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • C. Robert Matthews
    • 1
  • Edward P. Garvey
    • 2
  • Jonathan Swank
    • 3
  1. 1.Department of ChemistryPennsylvania State UniversityUniversity ParkUSA
  2. 2.Division of Experimental TherapyBurroughs-Wellcome CorporationResearch Triangle ParkUSA
  3. 3.Medical College of PennsylvaniaPhiladelphiaUSA

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