Secure CheckoutPersonal information is secured with SSL technology.
Free ShippingFree global shipping
No minimum order.
Purification and Characterization: R.R. Burgess, Use of Polyethyleneimine in Purification of DNA Binding Proteins. J.T. Kadonaga, Purification of Sequence-Specific Binding Proteins by DNA Affinity Chromatography. T. Formosa, J. Barry, B.M. Alberts, and J. Greenblatt, Using Protein Affinity Chromatography to Probe Structure of Protein Machines. D.L. Merkle and J.M. Berg, Metal Requirements for Nucleic Acid Binding Proteins. K. Tovar and W. Hillen, Large-Scale Preparation of DNA Fragments for Physical Studies of Protein Binding. G. P~aaarraga and R.E. Klevit, Multidimensional Nuclear Magnetic Resonance Spectroscopy DNA-Binding Proteins. A. Joachimiak and P.B. Sigler, Crystallization of Protein-DNA Complexes. DNA Binding and Bending: J. Carey, Gel Retardation. D.M. Crothers, M.R. Gartenberg, and T.E. Shrader, DNA Bending in Protein-DNA Complexes. S. Sasse-Dwight and J.D. Gralla, Footprinting Protein-DNA Complexes in Vivo. M. Dodson and H. Echols, Electron Microscopy of Protein-DNA Complexes. W.A. Lim, R.T. Sauer, and A.D. Lander, Analysis of DNA-Protein Interactions by Affinity Coelectrophoresis. J.W. Hockensmith, W.L. Kubasek, W.R. Vorachek, E.M. Evertsz, and P.H. von Hippel, Laser Cross-Linking Protein-Nucleic Acid Complexes. M. Buckle, A. Fritsch, P. Roux, J. Geiselmann, and H. Buc, Kinetic Studies on Promoter-RNA Polymerase Complexes. T.M. Lohman and W. Bujalowski, Thermodynamic Methods for Model-Independent Determination of Equilibrium Binding Isotherms for Protein-DNA Interactions: Spectroscopic Approaches to Monitor Binding. M.T. Record, Jr., J.-H. Ha, and M.A. Fisher, Analysis of Equilibrium and Kinetic Measurements to Determine Thermodynamic Origins of Stability and Specificity and Mechanism of Formation of Site-Specific Complexes between Proteins and Helical DNA. A. Hochschild, Detecting Cooperative Protein-DNA Interactions and DNA Loop Formation by Footprinting. Biochemical Analysis of Protein-Nucleic DNA Interactions: A. Wissmann and W. Hillen, DNA Contacts Probed by Modification Protection and Interference Studies. W.J. Dixon, J.J. Hayes, J.R. Levin, M.F. Weidner, B.A. Dombroski, and T.D. Tullius, Hydroxyl Radical Footprinting. D.S. Sigman, M.D. Kuwabara, C.-H.B. Chen, and T.W. Brucie, Nuclease Activity of 1,10-Phenanthroline-Copper in Study of Protein-DNA Interactions. C.R. Aiken and R.I. Gumport, Base Analogs in the Study of Restriction Enzyme-DNA Interactions. G.D. Stormo, Probing Information Content of DNA-Binding Sites. K.S. Matthews, A.E. Chakerian, and J.A. Gardner, Protein Chemical Modification as Probe of Structure-Function Relationships. P.B. Dervan, Characterization of Protein-DNA Complexes by Affinity Cleaving. K.R. Williams and W.H. Konigsberg, Identification of Amino Acid Residues at Interface of Protein-Nucleic Acid Complexes by Photochemical Cross-Linking. Genetic Analysis of Structure-Function Relationships: J.H. Miller, Use of Nonsense Suppression to Generate Altered Proteins. J.F. Reidhaar-Olson, J.U. Bowie, R.M. Breyer, J.C. Hu, K.L. Knight, W.A. Lim, M.C. Mossing, D.A. Parsell, K.R. Shoemaker, and R.T. Sauer, Random Mutagenesis of Protein Sequences Using Oligonucleotide Cassettes. S.P. Goff and V.R. Prasad, Linker Insertion Mutagenesis as Probe of Structure-Function Relationships. M.C. Mossing, J.U. Bowie, and R.T. Sauer, A Streptomycin Selection for DNA-Binding Activity. R.H. Ebright, Identification of Amino Acid-Base Pair Contacts by Genetic Methods. D.L. Oxender and A.L. Gibson, Second-Site Reversion as Means of Enhancing DNA-Binding Affinity. Author Index. Subject Index. Chapter References.
Methods widely used in the study of DNA binding proteins are presented in this volume. These include purification and protein characterization, assays of protein-DNA binding and protein-induced bending, and biochemical and genetic methods for probing the structure, energy, and specificity of protein-DNA interactions.
Biochemists, geneticists, molecular biologists, cell biologists, microbiologists, genetic engineers, analytical chemists, biophysicists, and industrial researchers working on protein products.
- No. of pages:
- © Academic Press 1991
- 11th December 1991
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Massachusetts Institute of Technology, Cambridge, Massachusetts, U.S.A.
Elsevier.com visitor survey
We are always looking for ways to improve customer experience on Elsevier.com.
We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit.
If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website.
Thanks in advance for your time.