Structure and Dynamics of Macromolecules: Absorption and Fluorescence StudiesStructure 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 |
Contents
| 1 | |
Principles and observables | 55 |
Descriptions and properties | 99 |
4 Fluorescence quenching | 141 |
5 Fluorescence polarization | 193 |
6 Förster energy transfer | 217 |
7 Origin of proteins fluorescence | 237 |
8 Description of the structure and dynamics of α1acid glycoprotein by
fluorescence studies | 261 |
9 Structure and dynamics of hemoglobin subunits and of myoglobin | 345 |
10 Fluorescence fingerprints of animal and vegetal species and or varieties | 373 |
| 387 | |
| 409 | |
Other editions - View all
Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies J.R. Albani No preview available - 2005 |
Common terms and phrases
0.1-acid glycoprotein absence absorption spectrum acid glycoprotein Albani amino acids Authorization of reprint binding Biochemistry calcofluor white calculated carbohydrate carbohydrate residues complex conformational crystal cytochrome cytochrome by core denaturation diffusion dipole dissociation constant domain dynamics Eisenia electron transfer emission maximum emission spectra emission wavelength energy transfer environment equal equation excitation wavelength Figure flavocytochrome fluorescence anisotropy fluorescence emission spectra fluorescence excitation spectrum fluorescence intensity quenching fluorescence quenching fluorescence spectra fluorophore function global heme heme pocket hemin hemoglobin hydrophobic increase indicates interaction Journal ligand measured microenvironment modification molecular molecule motions mutant myoglobin observed obtained occurs ol-acid optical density oxygen parameters peak peptide Perrin plot photon polarization porphyrin presence probe progesterone protein protein matrix protoporphyrin quantum yield quencher reprint accorded result rotamers rotational correlation shift sialic acid sialylated solvent Source structure studies temperature thermal Trp residues tryptophan tryptophan residues tyrosine Wavelength nm
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