Statistical Mechanics, Protein Structure, and Protein Substrate Interactions:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Boston, MA
Springer US
1994
|
| Schriftenreihe: | NATO ASI Series, Series B: Physics
325 |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Beschreibung: | A number of factors have come together in the last couple of decades to define the emerging interdisciplinary field of structural molecular biology. First, there has been the considerable growth in our ability to obtain atomic-resolution structural data for biological molecules in general, and proteins in particular. This is a result of advances in technique, both in x-ray crystallography, driven by the development of electronic detectors and of synchrotron radiation x-ray sources, and by the development ofNMR techniques which allow for inference of a three-dimensional structure of a protein in solution. Second, there has been the enormous development of techniques in DNA engineering which makes it possible to isolate and clone specific molecules of interest in sufficient quantities to enable structural measurements. In addition, the ability to mutate a given amino acid sequence at will has led to a new branch of biochemistry in which quantitative measurements can be made assessing the influence of a given amino acid on the function of a biological molecule. A third factor, resulting from the exponential increase in computing power available to researchers, has been the emergence of a growing body of people who can take the structural data and use it to build atomic-scale models of biomolecules in order to try and simulate their motions in an aqueous environment, thus helping to provide answers to one of the most basic questions of molecular biology: the relation of structure to function |
| Beschreibung: | 1 Online-Ressource (IX, 406 p) |
| ISBN: | 9781489913494 9781489913517 |
| ISSN: | 0258-1221 |
| DOI: | 10.1007/978-1-4899-1349-4 |
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Datensatz im Suchindex
| _version_ | 1804153075444744192 |
|---|---|
| any_adam_object | |
| author | Doniach, Sebastian |
| author_facet | Doniach, Sebastian |
| author_role | aut |
| author_sort | Doniach, Sebastian |
| author_variant | s d sd |
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| dewey-ones | 571 - Physiology & related subjects |
| dewey-raw | 571.1 |
| dewey-search | 571.1 |
| dewey-sort | 3571.1 |
| dewey-tens | 570 - Biology |
| discipline | Physik Biologie |
| doi_str_mv | 10.1007/978-1-4899-1349-4 |
| format | Electronic eBook |
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| id | DE-604.BV042412528 |
| illustrated | Not Illustrated |
| indexdate | 2024-07-10T01:20:50Z |
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| isbn | 9781489913494 9781489913517 |
| issn | 0258-1221 |
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| spelling | Doniach, Sebastian Verfasser aut Statistical Mechanics, Protein Structure, and Protein Substrate Interactions edited by Sebastian Doniach Proceedings of a NATO ARW held in Cargese, Corsica, France, June 1-5, 1993 Boston, MA Springer US 1994 1 Online-Ressource (IX, 406 p) txt rdacontent c rdamedia cr rdacarrier NATO ASI Series, Series B: Physics 325 0258-1221 A number of factors have come together in the last couple of decades to define the emerging interdisciplinary field of structural molecular biology. First, there has been the considerable growth in our ability to obtain atomic-resolution structural data for biological molecules in general, and proteins in particular. This is a result of advances in technique, both in x-ray crystallography, driven by the development of electronic detectors and of synchrotron radiation x-ray sources, and by the development ofNMR techniques which allow for inference of a three-dimensional structure of a protein in solution. Second, there has been the enormous development of techniques in DNA engineering which makes it possible to isolate and clone specific molecules of interest in sufficient quantities to enable structural measurements. In addition, the ability to mutate a given amino acid sequence at will has led to a new branch of biochemistry in which quantitative measurements can be made assessing the influence of a given amino acid on the function of a biological molecule. A third factor, resulting from the exponential increase in computing power available to researchers, has been the emergence of a growing body of people who can take the structural data and use it to build atomic-scale models of biomolecules in order to try and simulate their motions in an aqueous environment, thus helping to provide answers to one of the most basic questions of molecular biology: the relation of structure to function Life sciences Animal Physiology Life Sciences Biophysics and Biological Physics Biowissenschaften Konformation (DE-588)4164965-5 gnd rswk-swf Proteine (DE-588)4076388-2 gnd rswk-swf Proteinfaltung (DE-588)4324567-5 gnd rswk-swf Chemische Struktur (DE-588)4009857-6 gnd rswk-swf 1\p (DE-588)1071861417 Konferenzschrift 1993 Cargèse gnd-content Proteine (DE-588)4076388-2 s Chemische Struktur (DE-588)4009857-6 s 2\p DE-604 Konformation (DE-588)4164965-5 s 3\p DE-604 Proteinfaltung (DE-588)4324567-5 s 4\p DE-604 https://doi.org/10.1007/978-1-4899-1349-4 Verlag Volltext 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 2\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 3\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 4\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| spellingShingle | Doniach, Sebastian Statistical Mechanics, Protein Structure, and Protein Substrate Interactions Life sciences Animal Physiology Life Sciences Biophysics and Biological Physics Biowissenschaften Konformation (DE-588)4164965-5 gnd Proteine (DE-588)4076388-2 gnd Proteinfaltung (DE-588)4324567-5 gnd Chemische Struktur (DE-588)4009857-6 gnd |
| subject_GND | (DE-588)4164965-5 (DE-588)4076388-2 (DE-588)4324567-5 (DE-588)4009857-6 (DE-588)1071861417 |
| title | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions |
| title_alt | Proceedings of a NATO ARW held in Cargese, Corsica, France, June 1-5, 1993 |
| title_auth | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions |
| title_exact_search | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions |
| title_full | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions edited by Sebastian Doniach |
| title_fullStr | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions edited by Sebastian Doniach |
| title_full_unstemmed | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions edited by Sebastian Doniach |
| title_short | Statistical Mechanics, Protein Structure, and Protein Substrate Interactions |
| title_sort | statistical mechanics protein structure and protein substrate interactions |
| topic | Life sciences Animal Physiology Life Sciences Biophysics and Biological Physics Biowissenschaften Konformation (DE-588)4164965-5 gnd Proteine (DE-588)4076388-2 gnd Proteinfaltung (DE-588)4324567-5 gnd Chemische Struktur (DE-588)4009857-6 gnd |
| topic_facet | Life sciences Animal Physiology Life Sciences Biophysics and Biological Physics Biowissenschaften Konformation Proteine Proteinfaltung Chemische Struktur Konferenzschrift 1993 Cargèse |
| url | https://doi.org/10.1007/978-1-4899-1349-4 |
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