Proč už nepodporujeme prohlížeč Internet Explorer
Prohlížeč Internet Explorer již nepodporujeme a také důrazně nedoporučujeme, protože dlouhodobě funguje bez zásadních aktualizací, vylepšení a podpory. Obsahuje řadu závažných bezpečnostních rizik, které mohou způsobit únik citlivých informací a vašich osobních dat. Nehledě k tomu, že prohlížení a práce s webovými stránkami je v něm pomalejší až o 50 % v porovnání s ostatními prohlížeči.
Které prohlížeče tedy používat a kde si je můžete stáhnout?
Změna prohlížeče je jednoduchá, nezabere vám moc času a my vám s ní pomůžeme. Nachystali jsme pro vás seznam doporučených prohlížečů.
Vyberte si prohlížeč a klikněte na jeho název. Otevře se vám stránka, na které si prohlížeč můžete bezpečně nainstalovat.
TIP: Klidně si můžete nainstalovat všechny a vyzkoušet si, jak se vám s nimi pracuje.
A nebojte se, že změnou přijdete o všechny záložky, historii a uložená hesla. Můžete si je totiž jednoduše přenést. Postup pro dva nejpoužívanější prohlížeče přidáváme.
Doporučené prohlížeče:
Mozilla Firefox je výkonný, stabilní a bezpečný prohlížeč. Záložky a další data si můžete přenést podle návodu zde.
https://www.mozilla.org/cs/firefox/
https://support.mozilla.org/cs/kb/import-zalozek-dalsich-dat-z-internet-exploreru-ne
Google Chrome je rychlý, jednoduchý a bezpečný prohlížeč. Podívejte se na návod, jak přenést záložky a ostatní informace do Google Chrome.
https://www.google.com/intl/cs_ALL/chrome/security/
https://support.google.com/chrome/answer/96816?hl=cs
Už roztok chloridu guanidného je zvláštní. Lze v něm běžně nalézt guanidné kationty v přímém kontaktu, což je přinejmenším z pohledu elektrostatiky nepřirozené. Pro proteiny jsou účinky koncentrovaných roztoků zničující, po močovině se jedná o druhé nejběžnější denaturační činidlo. V tomto článku autoři ukazují, že existují tři způsoby účinku guanidných solí, stabilizující i destabilizující, které vždy souvisí s volbou aniontu. Tato práce je kombinací spektroskopických a termodynamických experimentů, počítačových simulací a termodynamického modelování.
Proč jsou některé soli účinnější při srážení proteinů, než jiné? Proč lze stejné pořadí účinnosti solí nalézt v celé plejádě fyzikálně-chemických vlastností a dějů? V tomto článku shrnujeme poznání, které vyplynulo z kombinace termodynamických a spektroskopických technik s počítačovým modelováním a teorií v posledních 10 letech, a přinášíme odpovědi na výše položené otázky. Článek byl publikován jako Feature Article v JPCB.
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p\u011bkn\u00e9 \u010dl\u00e1nky o interakci iont\u016f s biomolekulami","odkaz":"","targetblank":false,"detail":"<h2 class=\"articleTitle\"><span class=\"hlFld-Title\"><a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/jacs.6b11082\" target=\"_blank\">Guanidinium can both Cause and Prevent the Hydrophobic Collapse of Biomacromolecules<\/a><\/span><\/h2>\r\n<p><span style=\"font-size: small;\"><span style=\"font-size: 10pt;\"><span style=\"font-size: small;\">U\u017e roztok chloridu guanidn\u00e9ho je zvl\u00e1\u0161tn\u00ed. Lze v n\u011bm b\u011b\u017en\u011b <br \/> nal\u00e9zt guanidn\u00e9 kationty v p\u0159\u00edm\u00e9m kontaktu, co\u017e je p\u0159inejmen\u0161\u00edm z <br \/> pohledu elektrostatiky nep\u0159irozen\u00e9. Pro proteiny jsou \u00fa\u010dinky <br \/> koncentrovan\u00fdch roztok\u016f zni\u010duj\u00edc\u00ed, po mo\u010dovin\u011b se jedn\u00e1 o druh\u00e9 <br \/> nejb\u011b\u017en\u011bj\u0161\u00ed denatura\u010dn\u00ed \u010dinidlo. <a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/jacs.6b11082\" target=\"_blank\">V tomto \u010dl\u00e1nku<\/a> auto\u0159i ukazuj\u00ed, \u017ee existuj\u00ed <br \/> t\u0159i zp\u016fsoby \u00fa\u010dinku guanidn\u00fdch sol\u00ed, stabilizuj\u00edc\u00ed i destabilizuj\u00edc\u00ed, <br \/> kter\u00e9 v\u017edy souvis\u00ed s volbou aniontu. Tato pr\u00e1ce je kombinac\u00ed <br \/> spektroskopick\u00fdch a termodynamick\u00fdch experiment\u016f,\u00a0 po\u010d\u00edta\u010dov\u00fdch simulac\u00ed <br \/> a termodynamick\u00e9ho modelov\u00e1n\u00ed.<\/span><\/span><\/span><\/p>\r\n<h2 class=\"articleTitle\"><span class=\"hlFld-Title\"><a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/acs.jpcb.6b10797\" target=\"_blank\">Beyond the Hofmeister Series: Ion Specific Effects on Proteins and Their Biological Functions<\/a><\/span><\/h2>\r\n<p><img src=\"\/images\/215%210\/uzel\/0037758\/0001%7E%7Ec0tNLCktSk2J98hPy03NLC5JLYoP8XcGAA.png\" class=\"\" alt=\"Featured_Hofmeister_TOC (\u0161\u00ed\u0159ka 215px)\" width=\"215\" height=\"116\" \/><\/p>\r\n<p><img src=\"\/images\/215!0\/uzel\/0037758\/0002~~c0tNLCktSo33yE_LTc0sLkktik_OLwOSiUUl8VkFyUkA.png\" class=\"\" alt=\"Feature_Hofmeister_cover_art_jpcb (\u0161\u00ed\u0159ka 215px)\" width=\"215\" height=\"285\" \/><\/p>\r\n<p><span style=\"font-size: small;\"><span style=\"font-size: 10pt;\">Pro\u010d jsou n\u011bkter\u00e9 soli \u00fa\u010dinn\u011bj\u0161\u00ed p\u0159i sr\u00e1\u017een\u00ed protein\u016f, ne\u017e <br \/> jin\u00e9? Pro\u010d lze stejn\u00e9 po\u0159ad\u00ed \u00fa\u010dinnosti\u00a0 sol\u00ed nal\u00e9zt v cel\u00e9 plej\u00e1d\u011b <br \/> fyzik\u00e1ln\u011b-chemick\u00fdch vlastnost\u00ed a d\u011bj\u016f? 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