<BODY><IMG ALIGN=Left SRC="bits/Craigm2.gif" WIDTH=237 ALT="Photo of CTM"> <H4>Research Overview - Craig T. Martin</H4> Research carried out in our laboratory aims to use a variety of simple, yet very powerful tools of chemistry to understand relatively complex enzyme systems. <P>In studies of <A HREF = "t7rp/CmartinT7RP.html">structure and mechanism in the initiation of transcription</A>, the chemical synthesis of DNA oligonucleotides provides a powerful tool to probe individual chemical contacts along the surface of the DNA. Kinetic and thermodynamic studies of the effects of these simple mutation provide insight into not only the important contacts on the DNA, but also the roles that specific chemical interactions play in directing the RNA polymerase to initiate synthesis of RNA at a unique sequence in the DNA. <P>We have recently identified a central "core" within the promoter which is responsible for tight binding to the RNA polymerase. Energy from this interaction appears to be used to drive melting of the DNA near the start site. Other recent results have yielded unexpected (and therefore very intersting!) results, providing information on how the polymerase directs the initiating bases of the DNA template strand into the protein active site. <HR><A HREF="Pubs/CTMPublics.htm">Publication List</A><P> <A HREF = "#TopOfPage">Return to top of page</A><P> EMail: <A HREF="mailto:CMartin@Chem.UMass.edu">CMartin@Chem.UMass.edu</A></BODY>