STRUCTURE AND DYNAMICS OF MACROMOLECULES: ABSORPTION AND FLUORESCENCE STUDIES
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By J.R. Albani, Laboratoire de Biophysique Moleculairé, Universit des Sciences et Technologies de Lille, France
Description Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies is clearly written and contains invaluable
examples, coupled with illustrations that demonstrate a comprehensible analysis and presentation of the data. This book offers practical
information on the fundamentals of absorption and fluorescence, showing that it is possible to interpret the same result in different
ways. It is an asset to students, professors and researchers wishing to discover or use absorption and fluorescence spectroscopy, and
to scientists working on the structure and dynamics of macromolecules.
Audience
Academic and institutional libraries, government laboratories and scientists working in absorption and fluorescence spectroscopy, and on the structure and dynamics of macromolecules
Contents
Light absorption by a molecule
Jablonski diagram or diagram of electronic transitions.
Singlet and triplet states.
Forbidden and non forbidden transitions.
Reading
the Jablonski diagram.
Chemical bonds.
Absorption
Spectroscopy.
Fluorescence: Principles and observables
Fluorescence properties.
Fluorophores:
Descriptions and properties.
Types of fluorophores.
Effect of the environment on the fluorescence observables.
Fluorescence quenching
Collisional quenching: the Stern-Volmer
relation. The different types of dynamic quenching.
Static quenching.
Comparison between dynamics and static quenching.
Combination of dynamic and static quenching.
Thermal intensity quenching. Photoquenching.
Fluorescence polarization
Aim and definition. Principles of polarization or of photoselection.
Absorption transitions
and excitation polarization spectrum. Fluorescence depolarization.
Fluorescence anisotropy
decay time.
Depolarization and energy transfer.
Forster energy transfer
Principles.
Energy transfer parameters.
Relation between energy transfer and static quenching.
Origin of protein fluorescence
Description of the structure and dynamics of α1- acid glycoprotein by fluorescence studies
Methods. Fluorescence
properties of TNS bound to sialylated α1-acid.
Fluorescence properties of calcofluor bound to α1-acid
glycoprotein.
Fluorescence properties of the Trp residues in α1-acid glycoprotein.
F rster energy transfer experiments from Trp residues to calcofluor white.
Relation between the secondary structure
of carbohydrate residues of α1-acid glycoprotein and the fluorescence of the Trp residues of the protein.
Effect of the secondary structure of carbohydrate residues of α1-acid glycoprotein on the local
dynamics of the protein.
Tertiary structure of α1-acid glycoprotein: first model describing the presence of a pocket.
Are there any other alternative fluorescence methods other than the QREA or the Weber's method
to put into evidence the presence of a pocket within α1-acid glycoprotein?
Experiments giving proofs of the presence of a pocket within α1-acid glycoprotein.
Homology modeling of α1-
acid glycoprotein.
Dynamics of Trp residues in crystals of human α1- acid glycoprotein.
Structural
studies of human α1-acid glycoprotein followed by X-rays scattering and transmission electron microscopy.
Structure
and dynamics of hemoglobin subunits and of myoglobin
Dynamics of Trp residues in hemoglobin and in its subunits.
Properties of tprotoporphyrin IX in different solvents and in apomyoglobin.
Dynamics of protoporphyrin IX embedded in the heme.
Dynamics of the protein matrix and the heme pocket.
Significance of
the upward curvature.
Effect of sucrose on the bimolecular diffusion constant.
Fluorescence fingerprints of animal and vegetal species and/or varieties
Fluorescence fingerprints of Eisenia
fetida and Eisenia andrei.
Structural characterization of varieties of crops among a species
and of genetically modified organisms: a fluorescence study.
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