DNA Repair Enzymes: Structure, Biophysics, and Mechanism

Nonfiction, Science & Nature, Science, Other Sciences, Molecular Biology, Biological Sciences, Biochemistry, Health & Well Being, Medical
Cover of the book DNA Repair Enzymes: Structure, Biophysics, and Mechanism by Brandt Eichman, Elsevier Science
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Author: Brandt Eichman ISBN: 9780128125168
Publisher: Elsevier Science Publication: July 11, 2017
Imprint: Academic Press Language: English
Author: Brandt Eichman
ISBN: 9780128125168
Publisher: Elsevier Science
Publication: July 11, 2017
Imprint: Academic Press
Language: English

DNA Repair Enzymes, Part B, Volume 592 is the latest volume in the Methods in Enzymology series and the first part of a thematic that focuses on DNA Repair Enzymes. Topics in this updated volume include MacroBac: New Technologies for Robust and Efficient Large-Scale Production of Recombinant Multiprotein Complexes, Production and Assay of Recombinant Multisubunit Chromatin Remodeling Complexes, Analysis of Functional Dynamics of Modular Multidomain Proteins by SAXS and NMR, the Use of Single-Cysteine Variants for Trapping Transient States in DNA Mismatch Repair, and Structural Studies of RNases H2 as an Example of Crystal Structure Determination of Protein-Nucleic Acid Complexes.

  • Includes contributions from leading authorities working in enzymology
  • Focuses on DNA repair enzymes
  • Informs and updates on all the latest developments in the field of enzymology
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DNA Repair Enzymes, Part B, Volume 592 is the latest volume in the Methods in Enzymology series and the first part of a thematic that focuses on DNA Repair Enzymes. Topics in this updated volume include MacroBac: New Technologies for Robust and Efficient Large-Scale Production of Recombinant Multiprotein Complexes, Production and Assay of Recombinant Multisubunit Chromatin Remodeling Complexes, Analysis of Functional Dynamics of Modular Multidomain Proteins by SAXS and NMR, the Use of Single-Cysteine Variants for Trapping Transient States in DNA Mismatch Repair, and Structural Studies of RNases H2 as an Example of Crystal Structure Determination of Protein-Nucleic Acid Complexes.

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