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Registro Completo |
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Biblioteca(s): |
Embrapa Instrumentação. |
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Data corrente: |
22/01/2003 |
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Data da última atualização: |
26/08/2013 |
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Autoria: |
BRAND, L.; JOHNSON, M. L. (ed.). |
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Afiliação: |
Department of biology and biophysics, McCollum-Prant Institute, Johns Hopkins University, Baltimore, Maryland.; Department of Pharmacology, University of Virginia, Health Center Charlottesville, Virginia. |
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Título: |
Fluorescence spectroscopy. |
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Ano de publicação: |
1997 |
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Fonte/Imprenta: |
San Diego: Academic Press, [1997]. |
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Páginas: |
xxix, 628 p.: il. |
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Série: |
(Methods in enzymology, 278). |
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ISBN: |
0-12-182179-X |
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Idioma: |
Inglês |
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Conteúdo: |
1. Fluorescence in biophysics: accomplishments and deficiencies; 2. Design of profluorescent protease substrates guided by exciton theory; 3. Picosencond fluorescence decay curves collected on millisecond time scale: direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions; 4. Time-resolved room temperature tryptophyan phosphorescence in proteins; 5. Fluorescence line narrowing spectroscopy: a tool for studying proteins; 6. Determination of ground-state dissociation constant by fluorescence spectroscopy; 7. 1La and 1Lb transitions of tryptophyan: applications of theory and experimental observations to fluorescence of proteins; 8. Enhancement of protein spectra with tryptophan analogs: fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions; 9. Time-resolved fluorescence of constrained tryptophan derivatives: implications for protein fluorescence; 10. Conformational heterogeneity in crystalline proteins: time-resolved fluorescence studies; 11. Fluorescence methods for studying equilibrium macromolecule-ligand interactions; 12. Fluorescence methods for studying kinetics of protein-folding reactions; 13. Intramolecular pyrene excimer fluorescence: a probe of proximity and proteins conformational change; 14. Long-lifetime metal-ligand complexes as probes in biophysics and clinical chemistry; 15. N-terminal modification of proteins for fluorescence measurements; 16. Fluorescence studies of zinc finger peptides and proteins; 17. Fluorescence assays for DNA cleavage; 18. Fluorescent nucleotide analogs: synthesis and applications; 19. Fluorescence approaches to study of protein-nucleic acid complexation; 20. Fluorescence resonance energy transfer as a probe of DNA structure and function; 21. Energy transfer methods for detecting molecular clusters on cell surfaces; 22. Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide; 23. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching; 24. Fluorescence probes for studying membrane heterogeneity; 25. Preparation of bifluorescent-labeled glycopeptides for glycoamidase assay; 26. Preparation of fluorescence-labeled neoglycolipids for ceramide glycanase assays; 27. Applications of fluorescence resonance energy transfer to structure and mechanisms of chloroplast ATP synthase; 28. Intrinsic fluorescence of hemoglobins and myoglobins; 29. Multiple-domain fluorescence lifetime data analysis; Author index; Subject index. Menos1. Fluorescence in biophysics: accomplishments and deficiencies; 2. Design of profluorescent protease substrates guided by exciton theory; 3. Picosencond fluorescence decay curves collected on millisecond time scale: direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions; 4. Time-resolved room temperature tryptophyan phosphorescence in proteins; 5. Fluorescence line narrowing spectroscopy: a tool for studying proteins; 6. Determination of ground-state dissociation constant by fluorescence spectroscopy; 7. 1La and 1Lb transitions of tryptophyan: applications of theory and experimental observations to fluorescence of proteins; 8. Enhancement of protein spectra with tryptophan analogs: fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions; 9. Time-resolved fluorescence of constrained tryptophan derivatives: implications for protein fluorescence; 10. Conformational heterogeneity in crystalline proteins: time-resolved fluorescence studies; 11. Fluorescence methods for studying equilibrium macromolecule-ligand interactions; 12. Fluorescence methods for studying kinetics of protein-folding reactions; 13. Intramolecular pyrene excimer fluorescence: a probe of proximity and proteins conformational change; 14. Long-lifetime metal-ligand complexes as probes in biophysics and clinical chemistry; 15. N-terminal modification of proteins for fluorescence measurements; 16. Fluorescence studi... Mostrar Tudo |
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Palavras-Chave: |
Biomolécula; Biomolecules; Espectroscopia; Fluorescence spectroscopy; Instrumentação; Medida; Optical technique. |
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Thesaurus Nal: |
data analysis; instrumentation; measurement. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 03286nam a2200277 a 4500
001 1028165
005 2013-08-26
008 1997 bl uuuu 00u1 u #d
020 $a0-12-182179-X
100 1 $aBRAND, L.
245 $aFluorescence spectroscopy.
260 $aSan Diego: Academic Press, [1997].$c1997
300 $axxix, 628 p.: il.
490 $a(Methods in enzymology, 278).
520 $a1. Fluorescence in biophysics: accomplishments and deficiencies; 2. Design of profluorescent protease substrates guided by exciton theory; 3. Picosencond fluorescence decay curves collected on millisecond time scale: direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions; 4. Time-resolved room temperature tryptophyan phosphorescence in proteins; 5. Fluorescence line narrowing spectroscopy: a tool for studying proteins; 6. Determination of ground-state dissociation constant by fluorescence spectroscopy; 7. 1La and 1Lb transitions of tryptophyan: applications of theory and experimental observations to fluorescence of proteins; 8. Enhancement of protein spectra with tryptophan analogs: fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions; 9. Time-resolved fluorescence of constrained tryptophan derivatives: implications for protein fluorescence; 10. Conformational heterogeneity in crystalline proteins: time-resolved fluorescence studies; 11. Fluorescence methods for studying equilibrium macromolecule-ligand interactions; 12. Fluorescence methods for studying kinetics of protein-folding reactions; 13. Intramolecular pyrene excimer fluorescence: a probe of proximity and proteins conformational change; 14. Long-lifetime metal-ligand complexes as probes in biophysics and clinical chemistry; 15. N-terminal modification of proteins for fluorescence measurements; 16. Fluorescence studies of zinc finger peptides and proteins; 17. Fluorescence assays for DNA cleavage; 18. Fluorescent nucleotide analogs: synthesis and applications; 19. Fluorescence approaches to study of protein-nucleic acid complexation; 20. Fluorescence resonance energy transfer as a probe of DNA structure and function; 21. Energy transfer methods for detecting molecular clusters on cell surfaces; 22. Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide; 23. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching; 24. Fluorescence probes for studying membrane heterogeneity; 25. Preparation of bifluorescent-labeled glycopeptides for glycoamidase assay; 26. Preparation of fluorescence-labeled neoglycolipids for ceramide glycanase assays; 27. Applications of fluorescence resonance energy transfer to structure and mechanisms of chloroplast ATP synthase; 28. Intrinsic fluorescence of hemoglobins and myoglobins; 29. Multiple-domain fluorescence lifetime data analysis; Author index; Subject index.
650 $adata analysis
650 $ainstrumentation
650 $ameasurement
653 $aBiomolécula
653 $aBiomolecules
653 $aEspectroscopia
653 $aFluorescence spectroscopy
653 $aInstrumentação
653 $aMedida
653 $aOptical technique
700 1 $aJOHNSON, M. L.
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Registro original: |
Embrapa Instrumentação (CNPDIA) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Soja. Para informações adicionais entre em contato com valeria.cardoso@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Soja. |
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Data corrente: |
10/01/2019 |
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Data da última atualização: |
10/01/2019 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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Autoria: |
POMARI-FERNANDES, A.; BUENO, A. de F.; DE BORTOLI, S. A.; FAVETTI, B. M. |
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Afiliação: |
UFFS; ADENEY DE FREITAS BUENO, CNPSO; FCA/UNESP; IAPAR. |
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Título: |
Dispersal capacity of the egg parasitoid Telenomus remus Nixon (Hymenoptera: Platygastridae) in maize and soybean crops. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Biological Control, v. 126, p. 158-168, 2018. |
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DOI: |
10.1016/j.biocontrol.2018.08.009 |
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Idioma: |
Inglês |
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Thesagro: |
Controle Biológico; Glycine Max; Milho; Parasitologia; Soja; Spodoptera Frugiperda; Zea Mays. |
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Thesaurus NAL: |
Biological control; Corn; Parasitoids; Soybeans. |
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Categoria do assunto: |
O Insetos e Entomologia |
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Marc: |
LEADER 00862naa a2200289 a 4500
001 2103504
005 2019-01-10
008 2018 bl uuuu u00u1 u #d
024 7 $a10.1016/j.biocontrol.2018.08.009$2DOI
100 1 $aPOMARI-FERNANDES, A.
245 $aDispersal capacity of the egg parasitoid Telenomus remus Nixon (Hymenoptera$bPlatygastridae) in maize and soybean crops.$h[electronic resource]
260 $c2018
650 $aBiological control
650 $aCorn
650 $aParasitoids
650 $aSoybeans
650 $aControle Biológico
650 $aGlycine Max
650 $aMilho
650 $aParasitologia
650 $aSoja
650 $aSpodoptera Frugiperda
650 $aZea Mays
700 1 $aBUENO, A. de F.
700 1 $aDE BORTOLI, S. A.
700 1 $aFAVETTI, B. M.
773 $tBiological Control$gv. 126, p. 158-168, 2018.
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