Membrane Binding of Peripheral Proteins and its Characterisation Applying Fluorescence Methods.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F02%3A54030097" target="_blank" >RIV/61388955:_____/02:54030097 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Membrane Binding of Peripheral Proteins and its Characterisation Applying Fluorescence Methods.

Popis výsledku v původním jazyce

Basically, the problem of membrane binding of peripheral proteins can be studied in two ways. On the one hand we can address the protein itself, using either intrinsic tryptophan fluorescence or dyelabelled protein, as typically employed in fluorescencerecovery after photobleaching experiments. On the other hand we can approach the binding event from the membrane side, studying solvent relaxation, fluorescence anisotropy or excimer formation of suitable membrane probes. For the case of the blood coagulation protein prothrombin and its fragment l the combined use of these fluorescence methods shows a slightly tighter binding of the fragment l portion in the case of the entire prothrombin molecule compared to the isolated fragment l while no evidence could be obtained for hydrophobic membrane binding sites in the ''non-fragment l'' part of prothrombin.

Název v anglickém jazyce

Membrane Binding of Peripheral Proteins and its Characterisation Applying Fluorescence Methods.

Popis výsledku anglicky

Basically, the problem of membrane binding of peripheral proteins can be studied in two ways. On the one hand we can address the protein itself, using either intrinsic tryptophan fluorescence or dyelabelled protein, as typically employed in fluorescencerecovery after photobleaching experiments. On the other hand we can approach the binding event from the membrane side, studying solvent relaxation, fluorescence anisotropy or excimer formation of suitable membrane probes. For the case of the blood coagulation protein prothrombin and its fragment l the combined use of these fluorescence methods shows a slightly tighter binding of the fragment l portion in the case of the entire prothrombin molecule compared to the isolated fragment l while no evidence could be obtained for hydrophobic membrane binding sites in the ''non-fragment l'' part of prothrombin.

Druh

C - Kapitola v odborné knize

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A032" target="_blank" >LN00A032: Struktura a dynamika komplexních molekulových systémů a biomolekul</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2002

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název knihy nebo sborníku

Recent Research Developments in Proteins.

ISBN

81-7895-063-4

Počet stran výsledku

11

Strana od-do

277-288

Počet stran knihy

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Název nakladatele

Transworld Research Network

Místo vydání

Trivandrum

Kód UT WoS kapitoly

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