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DNA-Protein Interactions

Principles and Protocols

  • G. Geoff Kneale

Part of the Methods in Molecular Biology™ book series (MIMB, volume 30)

Table of contents

  1. Front Matter
    Pages i-xv
  2. Benoît Lehlanc, Tom Moss
    Pages 1-10
  3. Willi Metzger, Hermann Heumann
    Pages 11-20
  4. Peter Schickor, Hermann Heumann
    Pages 21-32
  5. Peter Schickor, Hermann Heumann
    Pages 33-41
  6. Peter E. Shaw, A. Francis Stewart
    Pages 79-87
  7. Malcolm Buckle, Andrew A. Wavers
    Pages 113-123
  8. Iain Manfield, Peter G. Stockley
    Pages 125-139
  9. Peter E. Nielsen
    Pages 141-149
  10. Simon E. Plyte, G. GeoffKheale
    Pages 161-168
  11. Daniel G. Fox, G. GeoffKineale
    Pages 169-184
  12. Andrew F Worrall
    Pages 199-210
  13. Michael J. O’Donohue, G. GeoffKneale
    Pages 211-225
  14. Stefan I. Dimitrov, Tom Moss
    Pages 227-236
  15. Raker Meffert, Klaus Dose, Gabriele Rathgeber, Hans-Jochen SchÄfer
    Pages 237-250
  16. Peter G. Stockley
    Pages 251-262
  17. John D. Taylor, Alison J. Ackroyd, Stephen E. Halford
    Pages 263-279
  18. Mark L. Carpenter, G. Geof Kiteale
    Pages 313-325
  19. Mark L. Carpenter, G. Geoff Kneale
    Pages 339-345
  20. Rachel M. Conlin, Raymond S. Brown
    Pages 357-370
  21. Stephen E. Halford, John D. Taylor, Christian L. M. Vermote, I. Barry Vipond
    Pages 385-396
  22. Stephen Busby, Annie Kolb, Stephen Minchin
    Pages 397-411
  23. Berndt Miiller, Stephen C. West
    Pages 413-423
  24. Back Matter
    Pages 425-427

About this book

Introduction

The study of protein-nucleic acid interactions is currently one of the most rapidly growing areas of molecular biology. DNA binding proteins are at the very heart of the regulation and control of gene expression, replication, and recombination: Enzymes that recognize and either modify or cleave specific DNA sequences are equally important to the cell. Some of the techniques reported in this volume can be used to identify previously unknown DNA binding proteins from crude cell extracts. Virtually all are capable of giving direct information on the molecular basis of the interaction—the location of the DNA binding site; the strength and specificity of binding; the identities of individual groups on specific bases involved in binding; the specific amino acid residues of the protein that interact with the DNA; or the effects of protein binding on gross conformation and local structure of DNA. The recognition of DNA sequences by proteins is a complex phenomenon, involving specific hydrogen bonding contacts to the DNA bases ("direct readout") and/or interactions with the sugar-phos­ phate backbone ("indirect readout"). The latter interactions can also be highly specific because of sequence-dependent conformational changes in the DNA. In addition, intercalation of planar aromatic amino acid side-chains between the DNA bases can occur, most notably with single-stranded DNA binding proteins. Furthermore, when bound, many DNA binding proteins induce drastic structural changes in the DNA as an integral part of their function.

Editors and affiliations

  • G. Geoff Kneale
    • 1
  1. 1.School of Biological Sciences; University of PortsmouthPortsmouthUK

Bibliographic information

  • DOI https://doi.org/10.1385/0896032566
  • Copyright Information Humana Press 1994
  • Publisher Name Humana Press
  • eBook Packages Springer Protocols
  • Print ISBN 978-0-89603-256-9
  • Online ISBN 978-1-59259-517-4
  • Series Print ISSN 1064-3745
  • Series Online ISSN 1940-6029
  • Buy this book on publisher's site
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