Author/Editor		Poklar, Nataša; Maček, Peter; Vesnaver, Gorazd
Title		Comparison of the acid and alkaline pH conformational states of pore-forming protein, equinatoxin II, by means of CD-spectroscopy
Translated title		Primerjava kislih in bazičnih konformacijskih stanj "pore-forming" proteina, ekvinatoksina II, z uporabo CD-spektroskopije
Type		članek
Source		Acta Biol Slov
Vol. and No.		Letnik 43, št. 1-2
Publication year		2000
Volume		str. 37-9
Language		eng
Abstract		Acid and alkaline pH conformational states of Equinatoxin II (EqTxII) at 25 degrees C studied by means of CD-spectroscopy. It has been observed that at acid pH - 1 EqTxII exists in the state which is characterized by the lack of tertiary structure and preserved non-active secondary straucture and can be thus described as an acid intermediate (molten globule) state. Confirmation state of EqTxII similar to the one observed at acid pH was detected also at pH - 12. These observations suggest that at those very different pH values the conformation state of EqTxII may in fact be quite similar. The high pH intermediate state is not stable in wider pH range with increasing pH undergoes a further transition towards an increased alpha-helical secondary structure.
Summary		Kislinska in bazna konformacijska stanja ekvinatoksina (EqTxII) pri 25 stopinjah C smo proučevali z metodo CD-spektroskopije. Ugotovili smo, da se pri nizkem pH - 1 EqTxII nahaja v konformacijskem stanju, za katerega je značilno, da nima terciarne strukture in ima ohranjeno, vendar spremenjeno sekundarno strukturo. EqTxII se, torej nahaja v kislem intermediatnem (molten globule) stanju. Pri visokem pH - 12 EqTxII zavzame podobno konformacijsko stanje kot pri nizkem pH. Na osnovi teh opazovanj lahko zaključimo, da so konfomacijska stanja EqTxII pri različnih pH podobna. Bazično inducirano intermediatno stanje EqTxII ni stabilno v širšem pH območju in z nadaljnjim naraščanjem pH preide v stanje z večjo vsebnostjo alpha-helične strukture.
Descriptors		CNIDARIAN VENOMS SEA ANEMONES HYDROGEN-ION CONCENTRATION SPECTROSCOPY, NEAR-INFRARED PROTEIN CONFORMATION