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eBook Nuclear Magnetic Resonance of Paramagnetic Macromolecules (Nato Science Series C:) ePub

eBook Nuclear Magnetic Resonance of Paramagnetic Macromolecules (Nato Science Series C:) ePub

by G.N. la Mar

  • ISBN: 0792333489
  • Category: Biological Sciences
  • Subcategory: Math Science
  • Author: G.N. la Mar
  • Language: English
  • Publisher: Springer; 1995 edition (January 31, 1995)
  • Pages: 391
  • ePub book: 1699 kb
  • Fb2 book: 1551 kb
  • Other: lrf docx mbr rtf
  • Rating: 4.9
  • Votes: 956

Description

Nato Science Series C. .

Nuclear Magnetic Resonance of Paramagnetic Macromolecules. Since A. Kowalsky's first report of the spectrum of cytochrome c in 1965, interest in the detection, assignment and interpretation of paramagnetic molecules has surged, especially in the last decade. Two classes of systems have played a key role in the development of the field: heme proteins and iron-sulfur proteins. These two systems are unique in many respects, one of which is that they contain well-defined chromophores, each of which can be studied in detail outside the protein matrix.

Series: Nato Science Series C: (Book 457). Hardcover: 391 pages. ISBN-13: 978-0792333487. Product Dimensions: . x . inches. Back to top. Get to Know Us. Careers.

Part of the NATO ASI Series book series (ASIC, volume 457). New Approaches to NMR of Paramagnetic Molecules. chromium cobalt iron lanthanum macromolecule metals protein proteins spectroscopy uranium. Claudio Luchinat, Mario Piccioli.

1995 Серия: Nato Science Series C: Язык: ENG Размер: 2. 9 x 1. 0 x . 9 cm Основная тема: Chemistry Рейтинг

Items related to Nuclear Magnetic Resonance of Paramagnetic Macromolecules. They are the most successfully studied macromolecules, and the first eight and last six of the seventeen contributions to this book deal with heme and/or iron-sulfur proteins.

Items related to Nuclear Magnetic Resonance of Paramagnetic Macromolecules. La Mar Nuclear Magnetic Resonance of Paramagnetic Macromolecules (NATO. The middle three chapters survey the progress on, and significant promise of, more difficult systems which do not possess a chromophore, but which have nevertheless yielded remarkable insights into their structure.

by Springer Science and Business Media LLC. in Nuclear Magnetic Resonance of Paramagnetic Macromolecules. Nuclear Magnetic Resonance of Paramagnetic Macromolecules pp 213-244; doi:10. The publisher has not yet granted permission to display this abstract.

Gerd . a Mar. Kowalsky's first report of the spectrum of cytochrome c in 1965, interest in the detection, assignment and interpretation of paramagnetic molecules has surged, especially in the last decade

Gerd . These two systems are unique in many respects, one of which is that they contain well-defined chromophores, each of which can be studied in detail outside the protein matrix

Workshop, Sintra, Portugal, June 4-8, 1994 Nuclear Magnetic Resonance of Paramagnetic Macromolecules. NATO Science Series C: (Closed).

NATO Science Series C: (Closed).

A nuclear magnetic resonance (NMR) gyroscope senses rotation as a shift in the Larmor frequency of nuclear magnetic moments as they precess about an applied field. A sensitive optically pumped magnetometer has been developed which can sense the weak magnetic fields associated with the nuclear moments and thus allow the detection and determination of the Larmor precession frequency. Atomic sensors have growing relevance to many facets of modern.

Since A. Kowalsky's first report of the spectrum of cytochrome c in 1965, interest in the detection, assignment and interpretation of paramagnetic molecules has surged, especially in the last decade. Two classes of systems have played a key role in the development of the field: heme proteins and iron-sulfur proteins. These two systems are unique in many respects, one of which is that they contain well-defined chromophores, each of which can be studied in detail outside the protein matrix. They are the most successfully studied macromolecules, and the first eight and last six of the seventeen contributions to this book deal with heme and/or iron-sulfur proteins. The middle three chapters survey the progress on, and significant promise of, more difficult systems which do not possess a chromophore, but which have nevertheless yielded remarkable insights into their structure.