Protein Stability and Folding: Theory and Practice
The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The developm...
Gespeichert in:
| Weitere Verfasser: | |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Totowa, NJ
Humana Press
1995
|
| Schriftenreihe: | Methods in Molecular Biology™
40 |
| Schlagworte: | |
| Online-Zugang: | UBR01 Volltext |
| Zusammenfassung: | The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The development of recombinant DNA techniques has made possible the production of large quantities of virtually any protein, as well as the production of proteins with altered amino acid sequence. Improvements in instrumentation, and the development and refinement of new techniques for studying these recombinant proteins, has been central to the progress made in this field. To give the reader adequate background information about the s- ject, the first two chapters of this book review two different, yet related, aspects of protein stability. The first chapter presents a review of our current understanding of the forces involved in determining the conf- mational stability of proteins as well as their three-dimensional folds. The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Although some techniques, such as X-ray crystallography and mass spectroscopy, are used in the study of protein stability, they are beyond the scope of this book and will not be covered extensively |
| Beschreibung: | 1 Online-Ressource (X, 377 p) |
| ISBN: | 9781592595273 |
| DOI: | 10.1385/0896033015 |
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Datensatz im Suchindex
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| dewey-full | 572 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
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| spelling | Protein Stability and Folding Theory and Practice edited by Bret A. Shirley Totowa, NJ Humana Press 1995 1 Online-Ressource (X, 377 p) txt rdacontent c rdamedia cr rdacarrier Methods in Molecular Biology™ 40 The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The development of recombinant DNA techniques has made possible the production of large quantities of virtually any protein, as well as the production of proteins with altered amino acid sequence. Improvements in instrumentation, and the development and refinement of new techniques for studying these recombinant proteins, has been central to the progress made in this field. To give the reader adequate background information about the s- ject, the first two chapters of this book review two different, yet related, aspects of protein stability. The first chapter presents a review of our current understanding of the forces involved in determining the conf- mational stability of proteins as well as their three-dimensional folds. The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Although some techniques, such as X-ray crystallography and mass spectroscopy, are used in the study of protein stability, they are beyond the scope of this book and will not be covered extensively Life Sciences Biochemistry, general Life sciences Biochemistry Proteinfaltung (DE-588)4324567-5 gnd rswk-swf Konformation (DE-588)4164965-5 gnd rswk-swf Methode (DE-588)4038971-6 gnd rswk-swf Proteine (DE-588)4076388-2 gnd rswk-swf 1\p (DE-588)4143413-4 Aufsatzsammlung gnd-content Proteinfaltung (DE-588)4324567-5 s Methode (DE-588)4038971-6 s DE-604 Proteine (DE-588)4076388-2 s Konformation (DE-588)4164965-5 s Shirley, Bret A. edt Erscheint auch als Druck-Ausgabe 9780896033016 https://doi.org/10.1385/0896033015 Verlag URL des Erstveröffentlichers Volltext 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| spellingShingle | Protein Stability and Folding Theory and Practice Life Sciences Biochemistry, general Life sciences Biochemistry Proteinfaltung (DE-588)4324567-5 gnd Konformation (DE-588)4164965-5 gnd Methode (DE-588)4038971-6 gnd Proteine (DE-588)4076388-2 gnd |
| subject_GND | (DE-588)4324567-5 (DE-588)4164965-5 (DE-588)4038971-6 (DE-588)4076388-2 (DE-588)4143413-4 |
| title | Protein Stability and Folding Theory and Practice |
| title_auth | Protein Stability and Folding Theory and Practice |
| title_exact_search | Protein Stability and Folding Theory and Practice |
| title_full | Protein Stability and Folding Theory and Practice edited by Bret A. Shirley |
| title_fullStr | Protein Stability and Folding Theory and Practice edited by Bret A. Shirley |
| title_full_unstemmed | Protein Stability and Folding Theory and Practice edited by Bret A. Shirley |
| title_short | Protein Stability and Folding |
| title_sort | protein stability and folding theory and practice |
| title_sub | Theory and Practice |
| topic | Life Sciences Biochemistry, general Life sciences Biochemistry Proteinfaltung (DE-588)4324567-5 gnd Konformation (DE-588)4164965-5 gnd Methode (DE-588)4038971-6 gnd Proteine (DE-588)4076388-2 gnd |
| topic_facet | Life Sciences Biochemistry, general Life sciences Biochemistry Proteinfaltung Konformation Methode Proteine Aufsatzsammlung |
| url | https://doi.org/10.1385/0896033015 |
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