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Linear Dichroism and Circular Dichroism: A Textbook on Polarized-Light Spectroscopy [Kõva köide]

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(Chalmers University of Technology, Sweden), (Warwick University, UK), (University of Birmingham, UK)
  • Formaat: Hardback, 304 pages, kõrgus x laius: 246x189 mm, kaal: 801 g, No
  • Ilmumisaeg: 02-Sep-2010
  • Kirjastus: Royal Society of Chemistry
  • ISBN-10: 1847559026
  • ISBN-13: 9781847559029
Teised raamatud teemal:
Linear Dichroism and Circular Dichroism: A Textbook on Polarized-Light SpectroscopySuurem pilt
  • Formaat: Hardback, 304 pages, kõrgus x laius: 246x189 mm, kaal: 801 g, No
  • Ilmumisaeg: 02-Sep-2010
  • Kirjastus: Royal Society of Chemistry
  • ISBN-10: 1847559026
  • ISBN-13: 9781847559029
Teised raamatud teemal:
Püsilink: https://www.kriso.ee/db/9781847559029.html
Märksõnad:
This book provides an introduction to optical anisotropy (linear dichroism, LD) and optical activity (circular dichroism, CD) as techniques for the study of structures and interactions of molecules in solution. The book covers the use of these techniques for both small and large molecular systems with particular emphasis being placed on proteins and nucleic acids. CD is a well-established technique and this book aims to explain how it can be used simply and effectively for new entrants to the field as well as covering more advanced techniques for experts. LD is often seen as a rather exotic method intended only for experienced spectroscopists. This book demonstrates that it is an approach with real utility that may be used by both students and scientists from graduate level onwards to give simple answers, which are not available from any other technique, to structural and kinetic questions. Much of the emphasis is on flow orientation of samples in solution phase. The book first describes the techniques and the information they can provide; it then goes on to give specific details on how to actually implement them, including a wide range of examples showing how LD and CD can help with * protein and nucleic acid secondary structure elucidation; * analysis of the formation and rearrangements of fibrous proteins and membrane proteins; * identification of the absolute configuration of small molecules; * determination of the orientation of small molecules in anisotropic media; * assignment of transition moment polarizations; * investigation of binding strengths and geometries of ligand-macromolecule complexes; * 3-D structure determination from LD, molecular replacement and MD modeling. The advantages of combined LD/CD studies are also outlined with examples of DNA/drug complexes and protein insertion into membranes. Taken together the book represents a comprehensive text on the theory and application of LD and CD in the chemical and biological sciences.
Chapter 1 Linear and circular dichroism spectroscopy: basic principles
1(14)
1.1 Introduction
2(1)
1.2 Electromagnetic radiation and spectroscopy
3(1)
1.3 Normal absorption spectroscopy
4(5)
1.4 Linear dichroism
9(3)
1.5 Circular dichroism
12(3)
Chapter 2 Spectroscopic practicalities
15(34)
2.1 Introduction
16(1)
2.2 Measuring linear dichroism spectra
16(3)
2.3 Molecular alignment techniques
19(14)
2.4 Experimental considerations for CD and LD spectroscopy
33(5)
2.5 Sample preparation for LD and CD spectroscopy
38(2)
2.6 Spectral artifacts
40(7)
2.7 Instrumentation considerations
47(2)
Chapter 3 Linear dichroism of biological macromolecules
49(28)
3.1 Introduction
50(1)
3.2 Qualitative analysis of LD
51(1)
3.3 Uniaxial orientation
52(1)
3.4 Reduced LD
53(1)
3.5 Nucleic acids
54(4)
3.6 LD of DNA-bound ligands
58(7)
3.7 Proteins
65(4)
3.8 Membrane proteins
69(4)
3.9 Fibrous proteins: cytoskeletal proteins
73(4)
Chapter 4 Circular dichroism of biological macromolecules
77(28)
4.1 Introduction
78(1)
4.2 Qualitative description of the origin of CD signals
78(2)
4.3 CD of polynucleotides: DNA and RNA
80(5)
4.4 DNA/ligand interactions
85(4)
4.5 CD of polypeptides and proteins
89(8)
4.6 Oriented CD
97(4)
4.7 CD of chiraldimers
101(4)
Chapter 5 Advanced LD methods for biological macromolecules
105(36)
5.1 Introduction
106(1)
5.2 DNA-ligand absorbance, LD and CD
106(1)
5.3 Liposome orientation
106(3)
5.4 Membrane peptides and proteins in liposomes
109(6)
5.5 DNA superstructures
115(1)
5.6 Protein-DNA interactions
115(4)
5.7 Site-specific LD spectroscopy: DNA binding of recombination enzymes
119(6)
5.8 Orientation of metal complexes bound to DNA
125(2)
5.9 Bacteriophage, a viral pathogen of bacteria
127(3)
5.10 Synchrotron radiation linear dichroism of DNAs
130(2)
5.11 DNA oriented on carbon nanotubes
132(2)
5.12 Peptidoglycan layer of bacterial cells
134(1)
5.13 LD of flow-oriented polymers
135(6)
Chapter 6 Linear dichroism of small molecules
141(26)
6.1 Introduction
142(1)
6.2 Some LD definitions
142(1)
6.3 Orientational and optical contributions to LD
143(3)
6.4 Uniaxial orientation
146(4)
6.5 Orientation triangle
150(2)
6.6 Determination of transition polarizations
152(8)
6.7 Determination of polarizations of overlapping transitions
160(1)
6.8 Resolution of angle-sign ambiguities
161(3)
6.9 LD of samples with a distribution of orientations
164(3)
Chapter 7 Molecular orientation principles
167(16)
7.1 Sample orientation for LD spectroscopy
168(1)
7.2 Equations for determination of molecular orientation
168(4)
7.3 Flow orientation of brain microtubules
172(3)
7.4 Derivation of the relationship between fluorescence anisotropy and transition polarization
175(2)
7.5 Orientation distributions
177(3)
7.6 Orientation of molecules bound to cylindrical bodies in shear flow
180(3)
Chapter 8 Analysis of circular dichroism: electric dipole allowed transitions
183(28)
8.1 Introduction
184(1)
8.2 Ways of analyzing CD
184(2)
8.3 Degenerate coupled-oscillator CD: general case
186(1)
8.4 Qualitative approach to exciton CD
187(2)
8.5 Quantitative approach to exciton CD
189(3)
8.6 Degenerate coupled-oscillator CD: some examples
192(7)
8.7 Non-degenerate coupled-oscillator CD: general case
199(2)
8.8 Non-degenerate coupled-oscillator CD: some examples
201(7)
8.9 CD of dimetallo helicates
208(3)
Chapter 9 Analysis of circular dichroism: magnetic dipole allowed transitions and magnetic CD
211(18)
9.1 Introduction
212(1)
9.2 Magnetic dipole allowed transitions
212(1)
9.3 n→Π carbonyl transition and the octant rule
213(3)
9.4 n→Π carbonyl transition and the dynamic coupling model: justification of the octant rule
216(4)
9.5 d-d transitions of transition metal complexes: symmetry dependence of the CD of mda transitions
220(4)
9.6 Magnetic circular dichroism
224(5)
Chapter 10 Circular dichroism formalism
229(28)
10.1 Introduction
230(1)
10.2 Beer-Lambert law
230(1)
10.3 Polarized light and spectropolarimeters
231(3)
10.4 Interaction of radiation with matter
234(4)
10.5 CD, transition moment operators, and transition moments
238(3)
10.6 CD from the coupling of degenerate electric dipole transition moments in identical chromophores: the degenerate coupled-oscillator model
241(3)
10.7 CD from the coupling of electric dipole transition moments in non-identical chromophores: the non-degenerate coupled-oscillator model
244(2)
10.8 Magnetic dipole allowed transitions: the dynamic coupling model
246(4)
10.9 Magnetic circular dichroism
250(5)
10.10 Multipole expansion of the interaction operator
255(2)
Chapter 11 Further derivations and definitions
257(16)
11.1 Vectors
258(2)
11.2 Relationship between isotropic and unpolarized absorbance
260(1)
11.3 Determination of equilibrium binding constants
261(5)
11.4 Momentum-dipole equivalence
266(2)
11.5 Definitions and units
268(2)
11.6 Dipole moments
270(3)
References 273(15)
Subject Index 288
Bengt NordÚn is a Professor of Physical Chemistry at the Chalmers University of Technology in Sweden. He has a BSc and PhD from the University of Lund and is renowned for pioneering linear dichroism spectroscopy for the study of transition moments, molecular interactions and macromolecular structures in solution. Alison Rodger is a Professor of Biophysical Chemistry in the Department of Chemistry at the University of Warwick. She has a BSc and a PhD from the University of Sydney and an MA from the University of Oxford. Timothy Dafforn has a BSc from the University of Cardiff and a PhD from the University of Bristol. He is a Lecturer at the University of Birmingham and a pioneer in the use of linear dichroism methods in the study of biological systems.