DNA-Protein Interactions: Principles and Protocols
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 spec...
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Weitere Verfasser: | |
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Format: | Elektronisch E-Book |
Sprache: | English |
Veröffentlicht: |
Totowa, NJ
Humana Press
1994
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Schriftenreihe: | Methods in Molecular Biology™
30 |
Schlagworte: | |
Online-Zugang: | UBR01 Volltext |
Zusammenfassung: | 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 |
Beschreibung: | 1 Online-Ressource (XV, 427 p) |
ISBN: | 9781592595174 |
DOI: | 10.1385/0896032566 |
Internformat
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Datensatz im Suchindex
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isbn | 9781592595174 |
language | English |
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spelling | DNA-Protein Interactions Principles and Protocols edited by G. Geoff Kneale Totowa, NJ Humana Press 1994 1 Online-Ressource (XV, 427 p) txt rdacontent c rdamedia cr rdacarrier Methods in Molecular Biology™ 30 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 Life Sciences Biochemistry, general Life sciences Biochemistry Proteine (DE-588)4076388-2 gnd rswk-swf Methode (DE-588)4038971-6 gnd rswk-swf Wechselwirkung (DE-588)4064937-4 gnd rswk-swf DNS (DE-588)4070512-2 gnd rswk-swf Proteine (DE-588)4076388-2 s DNS (DE-588)4070512-2 s Wechselwirkung (DE-588)4064937-4 s DE-604 Methode (DE-588)4038971-6 s Geoff Kneale, G. edt Erscheint auch als Druck-Ausgabe 9780896032569 https://doi.org/10.1385/0896032566 Verlag URL des Erstveröffentlichers Volltext |
spellingShingle | DNA-Protein Interactions Principles and Protocols Life Sciences Biochemistry, general Life sciences Biochemistry Proteine (DE-588)4076388-2 gnd Methode (DE-588)4038971-6 gnd Wechselwirkung (DE-588)4064937-4 gnd DNS (DE-588)4070512-2 gnd |
subject_GND | (DE-588)4076388-2 (DE-588)4038971-6 (DE-588)4064937-4 (DE-588)4070512-2 |
title | DNA-Protein Interactions Principles and Protocols |
title_auth | DNA-Protein Interactions Principles and Protocols |
title_exact_search | DNA-Protein Interactions Principles and Protocols |
title_full | DNA-Protein Interactions Principles and Protocols edited by G. Geoff Kneale |
title_fullStr | DNA-Protein Interactions Principles and Protocols edited by G. Geoff Kneale |
title_full_unstemmed | DNA-Protein Interactions Principles and Protocols edited by G. Geoff Kneale |
title_short | DNA-Protein Interactions |
title_sort | dna protein interactions principles and protocols |
title_sub | Principles and Protocols |
topic | Life Sciences Biochemistry, general Life sciences Biochemistry Proteine (DE-588)4076388-2 gnd Methode (DE-588)4038971-6 gnd Wechselwirkung (DE-588)4064937-4 gnd DNS (DE-588)4070512-2 gnd |
topic_facet | Life Sciences Biochemistry, general Life sciences Biochemistry Proteine Methode Wechselwirkung DNS |
url | https://doi.org/10.1385/0896032566 |
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