Secure CheckoutPersonal information is secured with SSL technology.
Free ShippingFree global shipping
No minimum order.
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.
- Offers concise information on the fundamentals of absorption and fluorescence
- Critically reviews examples taken from previously published literature
- Highly illustrated, it is suitable for academic and institutional libraries and government laboratories
Academic and institutional libraries, government laboratories and scientists working in absorption and fluorescence spectroscopy, and on the structure and dynamics of macromolecules
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.
Fluorescence: Principles and observables
Fluorophores: Descriptions and properties.
Types of fluorophores.
Effect of the environment on the fluorescence observables.
Collisional quenching: the Stern-Volmer relation.
The different types of dynamic quenching.
Comparison between dynamics and static quenching.
Combination of dynamic and static quenching.
Thermal intensity quenching.
Aim and definition.
Principles of polarization or of photoselection.
Absorption transitions and excitation polarization spectrum.
Fluorescence anisotropy decay time.
Depolarization and energy transfer.
Forster energy transfer
Energy transfer parameters.
Relation between energy transfer and static quenching.
Origin of protein fluorescence
Description of the structure and dynamics of &agr;1- acid glycoprotein by fluorescence studies
Fluorescence properties of TNS bound to sialylated &agr;1-acid.
Fluorescence properties of calcofluor bound to &agr;1-acid glycoprotein.
Fluorescence properties of the Trp residues in &agr;1-acid glycoprotein.
Förster energy transfer experiments from Trp residues to calcofluor white.
Relation between the secondary structure of carbohydrate residues of &agr;1-acid glycoprotein and the fluorescence of the Trp residues of the protein.
Effect of the secondary structure of carbohydrate residues of &agr;1-acid glycoprotein on the local dynamics of the protein.
Tertiary structure of &agr;1-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 &agr;1-acid glycoprotein?
Experiments giving proofs of the presence of a pocket within &agr;1-acid glycoprotein.
Homology modeling of &agr;1- acid glycoprotein.
Dynamics of Trp residues in crystals of human &agr;1- acid glycoprotein.
Structural studies of human &agr;1-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.
- No. of pages:
- © Elsevier Science 2004
- 17th September 2004
- Elsevier Science
- Hardcover ISBN:
- eBook ISBN:
Laboratoire de Biophysique Moleculairé, Université des Sciences et Technologies de Lille, France
Elsevier.com visitor survey
We are always looking for ways to improve customer experience on Elsevier.com.
We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit.
If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website.
Thanks in advance for your time.