Zur Startseite gehen
0,00 €*
Cover: 9780306464515 | Protein Fluorescence | Joseph R. Lacowicz | Buch | Englisch | 2000
Dekorationsartikel gehören nicht zum Leistungsumfang.
Protein Fluorescence
Buch von Joseph R. Lacowicz
Sprache: Englisch

141,95 €*

inkl. MwSt.

Versandkostenfrei per Post / DHL

Lieferzeit 2-3 Wochen

Kategorien:
Beschreibung
The intrinsic or natural fluorescence of proteins is perhaps the most complex area of biochemical fluorescence. Fortunately the fluorescent amino acids, phenylalanine, tyrosine and tryptophan are relatively rare in proteins. Tr- tophan is the dominant intrinsic fluorophore and is present at about one mole % in protein. As a result most proteins contain several tryptophan residues and even more tyrosine residues. The emission of each residue is affected by several excited state processes including spectral relaxation, proton loss for tyrosine, rotational motions and the presence of nearby quenching groups on the protein. Additionally, the tyrosine and tryptophan residues can interact with each other by resonance energy transfer (RET) decreasing the tyrosine emission. In this sense a protein is similar to a three-particle or mul- particle problem in quantum mechanics where the interaction between particles precludes an exact description of the system. In comparison, it has been easier to interpret the fluorescence data from labeled proteins because the fluorophore density and locations could be controlled so the probes did not interact with each other. From the origins of biochemical fluorescence in the 1950s with Prof- sor G. Weber until the mid-1980s, intrinsic protein fluorescence was more qualitative than quantitative. An early report in 1976 by A. Grindvald and I. Z. Steinberg described protein intensity decays to be multi-exponential. Attempts to resolve these decays into the contributions of individual tryp- phan residues were mostly unsuccessful due to the difficulties in resolving closely spaced lifetimes.
The intrinsic or natural fluorescence of proteins is perhaps the most complex area of biochemical fluorescence. Fortunately the fluorescent amino acids, phenylalanine, tyrosine and tryptophan are relatively rare in proteins. Tr- tophan is the dominant intrinsic fluorophore and is present at about one mole % in protein. As a result most proteins contain several tryptophan residues and even more tyrosine residues. The emission of each residue is affected by several excited state processes including spectral relaxation, proton loss for tyrosine, rotational motions and the presence of nearby quenching groups on the protein. Additionally, the tyrosine and tryptophan residues can interact with each other by resonance energy transfer (RET) decreasing the tyrosine emission. In this sense a protein is similar to a three-particle or mul- particle problem in quantum mechanics where the interaction between particles precludes an exact description of the system. In comparison, it has been easier to interpret the fluorescence data from labeled proteins because the fluorophore density and locations could be controlled so the probes did not interact with each other. From the origins of biochemical fluorescence in the 1950s with Prof- sor G. Weber until the mid-1980s, intrinsic protein fluorescence was more qualitative than quantitative. An early report in 1976 by A. Grindvald and I. Z. Steinberg described protein intensity decays to be multi-exponential. Attempts to resolve these decays into the contributions of individual tryp- phan residues were mostly unsuccessful due to the difficulties in resolving closely spaced lifetimes.
Über den Autor
Dr. J.R. Lakowicz is Professor of Biochemistry at the University of Maryland School of Medicine and Director of the Center for Fluorescence Spectroscopy. Dr. Lakowicz has published over 400 scientific articles, has edited numerous books, holds 16 issued patents, and is the sole author of the widely used text, Principles of Fluorescence Spectroscopy, also published by Kluwer Academic/Plenum Publishers, now in its Second Edition.
Inhaltsverzeichnis
Intrinsic Fluorescence of Proteins.- Spectral Enhancement of Proteins by in vivo Incorporation of Tryptophan Analogues.- Room Temperature Tryptophan Phosphorescence as a Probe of Structural and Dynamic Properties of Proteins.- Azurins and Their Site-Directed Mutants.- Barnase: Fluorescence Analysis of A Three Tryptophan Protein.- Fluorescence Study of the DsbA Protein from Escherichia Coli.- The Conformational Flexibility of Domain III of Annexin V is Modulated by Calcium, pH and Binding to Membrane/Water Interfaces.- Tryptophan Calmodulin Mutants.- Luminescence Studies with trp Aporepressor and Its Single Tryptophan Mutants.- Heme-Protein Fluorescence.- Conformation of Troponin Subunits and Their Complexes from Striated Muscle.- Fluorescence of Extreme Thermophilic Proteins.
Details
Erscheinungsjahr: 2000
Fachbereich: Theoretische Chemie
Genre: Chemie
Rubrik: Naturwissenschaften & Technik
Medium: Buch
Seiten: 336
Reihe: Topics in Fluorescence Spectroscopy
ISBN-13: 9780306464515
ISBN-10: 0306464519
Sprache: Englisch
Ausstattung / Beilage: HC runder Rücken kaschiert
Einband: Gebunden
Redaktion: Lacowicz, Joseph R.
Auflage: 2000
Hersteller: Springer US
Springer US, New York, N.Y.
Topics in Fluorescence Spectroscopy
Maße: 235 x 157 x 23 mm
Von/Mit: Joseph R. Lacowicz
Erscheinungsdatum: 30.11.2000
Gewicht: 0,641 kg
preigu-id: 102552901
Über den Autor
Dr. J.R. Lakowicz is Professor of Biochemistry at the University of Maryland School of Medicine and Director of the Center for Fluorescence Spectroscopy. Dr. Lakowicz has published over 400 scientific articles, has edited numerous books, holds 16 issued patents, and is the sole author of the widely used text, Principles of Fluorescence Spectroscopy, also published by Kluwer Academic/Plenum Publishers, now in its Second Edition.
Inhaltsverzeichnis
Intrinsic Fluorescence of Proteins.- Spectral Enhancement of Proteins by in vivo Incorporation of Tryptophan Analogues.- Room Temperature Tryptophan Phosphorescence as a Probe of Structural and Dynamic Properties of Proteins.- Azurins and Their Site-Directed Mutants.- Barnase: Fluorescence Analysis of A Three Tryptophan Protein.- Fluorescence Study of the DsbA Protein from Escherichia Coli.- The Conformational Flexibility of Domain III of Annexin V is Modulated by Calcium, pH and Binding to Membrane/Water Interfaces.- Tryptophan Calmodulin Mutants.- Luminescence Studies with trp Aporepressor and Its Single Tryptophan Mutants.- Heme-Protein Fluorescence.- Conformation of Troponin Subunits and Their Complexes from Striated Muscle.- Fluorescence of Extreme Thermophilic Proteins.
Details
Erscheinungsjahr: 2000
Fachbereich: Theoretische Chemie
Genre: Chemie
Rubrik: Naturwissenschaften & Technik
Medium: Buch
Seiten: 336
Reihe: Topics in Fluorescence Spectroscopy
ISBN-13: 9780306464515
ISBN-10: 0306464519
Sprache: Englisch
Ausstattung / Beilage: HC runder Rücken kaschiert
Einband: Gebunden
Redaktion: Lacowicz, Joseph R.
Auflage: 2000
Hersteller: Springer US
Springer US, New York, N.Y.
Topics in Fluorescence Spectroscopy
Maße: 235 x 157 x 23 mm
Von/Mit: Joseph R. Lacowicz
Erscheinungsdatum: 30.11.2000
Gewicht: 0,641 kg
preigu-id: 102552901
Warnhinweis

Ähnliche Produkte

Ähnliche Produkte

Buch
Cover: 9780387849225 | Solving the Pell Equation | Hugh Williams (u. a.) | Buch | XX | 2008
Solving the Pell Equation
EAN: 9780387849225
Sprache: Englisch
Von/Mit: Hugh Williams (u. a.)

51,95 €*

Lieferzeit 2-3 Wochen

Taschenbuch
Cover: 9783642417092 | Kekulés Träume | Eine andere Einführung in die Organische Chemie
Kekulés Träume
Eine andere Einführung in die Organische Chemie
EAN: 9783642417092
Sprache: Deutsch
Von/Mit: Dieter Neubauer

37,99 €*

Lieferzeit 4-7 Werktage

Taschenbuch
Cover: 9783319658667 | Foundations of Quantum Mechanics | Travis Norsen | Taschenbuch | 2017
Foundations of Quantum Mechanics
An Exploration of the Physical Meaning of Quantum Theory
EAN: 9783319658667
Sprache: Englisch
Von/Mit: Travis Norsen

58,20 €*

Lieferzeit 1-2 Wochen

Taschenbuch
Cover: 9780198755500 | Computational Chemistry | Jeremy Harvey | Taschenbuch | Englisch
Computational Chemistry
EAN: 9780198755500
Sprache: Englisch
Von/Mit: Jeremy Harvey

48,95 €*

Lieferzeit 1-2 Wochen

Buch
Cover: 9781891389566 | Mathematics for Physical Chemistry: Opening Doors | Opening Doors
Mathematics for Physical Chemistry: Opening Doors
EAN: 9781891389566
Sprache: Englisch
Von/Mit: Donald A. Mcquarrie

71,20 €*

Lieferzeit 1-2 Wochen

Buch
Cover: 9783527413683 | Halliday Physik für natur- und ingenieurwissenschaftliche Studiengänge
Halliday Physik für natur- und ingenieurwissenschaftliche Studiengänge
EAN: 9783527413683
Sprache: Deutsch
Von/Mit: David Halliday (u. a.)

59,90 €*

Lieferzeit 1-2 Werktage

Bundle
Cover: 9783609690810 | Sichere Lagerung gefährlicher Stoffe, m. 1 Buch, m. 1 Online-Zugang
Sichere Lagerung gefährlicher Stoffe, m. 1 Buch, m. 1 Online-Zugang
EAN: 9783609690810
Sprache: Deutsch
Von/Mit: Norbert Müller (u. a.)

64,99 €*

Lieferzeit 1-2 Werktage

Taschenbuch
Cover: 9783662646021 | Fit in Organik | Rudi Hutterer | Taschenbuch | Springer, Berlin
Fit in Organik
Das Prüfungstraining für alle Naturwissenschaftler und Mediziner
EAN: 9783662646021
Sprache: Deutsch
Von/Mit: Rudi Hutterer

54,99 €*

Lieferzeit 1-2 Werktage

Taschenbuch
Cover: 9780815344469 | How Proteins Work | Michael Williamson | Taschenbuch | Englisch | 2011
How Proteins Work
EAN: 9780815344469
Sprache: Englisch
Von/Mit: Michael Williamson

103,95 €*

Lieferzeit 1-2 Wochen

Taschenbuch
Cover: 9780226829562 | The Chemical Age | Frank A. von Hippel | Taschenbuch | Englisch | 2023
The Chemical Age
How Chemists Fought Famine and Disease, Killed Millions, and Changed Our Relationship with the Earth
EAN: 9780226829562
Sprache: Englisch
Von/Mit: Frank A. von Hippel

18,95 €*

Lieferzeit 1-2 Werktage

Taschenbuch
Cover: 9781398301559 | Cambridge Primary Science Workbook 6 Second Edition | Taschenbuch
Cambridge Primary Science Workbook 6 Second Edition
EAN: 9781398301559
Sprache: Englisch
Von/Mit: Andrea Mapplebeck (u. a.)
Maße: 290 x 204 x 6 mm
Empfohlen (von): 5

16,80 €*

Lieferzeit 1-2 Wochen

Diese Website verwendet Cookies, um eine bestmögliche Erfahrung bieten zu können. Mehr Informationen ...