Author/Editor		Jerala, Roman; Žerovnik, Eva
Title		Dimerization of human stefin A under partially denaturating conditions
Translated title		Dimerizacija humanega stefina A v delno denaturajočih razmerah
Type		članek
Source		Acta Biol Slov
Vol. and No.		Letnik 43, št. 1-2
Publication year		2000
Volume		str. 83-7
Language		eng
Abstract		Protein misfolding and aggregation have attracted great attention due to their involvement in conformational disease. We have observed that under partially denaturing conditions stefin A forms dimers, which are extremely stable can only be dissociated by denaturation. Assignation of backbonr amides of dimer and temperature dependence of hydrogen exchange of monomer and dimer indicate that the transition step in dimerization is largely unfolded. Results indicate that monometric stefin A is actually metastable under physiological concentrations.
Summary		Napačno zvitje proteinov in agregacija sta pomembna zaradi vloge pri t.i. "konformacijskih boleznih". Pod pogoji delne denaturacije smo opazili tvorbo dimerov stefina A, ki so izredno stabilni in jih lahko ločimo le z denaturacijo. Na podlagi asignacije amidnih skupin polipeptidnega ogrodja in temperaturne odvisnosti vodikove izmenjave dimera in monomera smo ugotovili, da je prehodno stanje tvorbe dimerov pretežno odvito. Rezultati kažejo, da je v fizioloških pogojih monomeren stefin A dejansko nestabilen.
Descriptors		DIMERIZATION CYSTEINE PROTEINASE INHIBITORS PROTEIN DENATURATION PROTEIN FOLDING PROTEIN CONFORMATION NUCLEAR MAGNETIC RESONANCE