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. 1 B), and most of the changes in anisotropy only took place between 2 and 5 M GdnHCl (Fig
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. The enzymatic activity was determined by measuring the absorbance at 238 nm accompanied with hydrolysis of the substrate and using the molar absorption coefficient ε^sub 238^ = 185 M^sup -1^cm^sup -1^ as reported by Kordel and Schneider (5,6), except that chloroacetyl-L-leucine was used instead of pure-L-enantiomorph
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. Each measurement was an average of three readings
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. Since the folding process is complex in multidomain proteins, where each domain may be able to refold independently and interdomain interactions may affect the overall folding process, EI can be used, in addition, as a model protein to improve our knowledge of protein folding and assembly of multidomain-oligomeric proteins
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. The sequences are 5' -Cy3 AAA UAG AGA AGC GAA CCA GAG AAA CAC ACG CC-3' (2WJ/3WJ/4WJ), 5'-Cy5 GGC GUG GUA CAU UAC CUG GUA CCC CCU CGC dAGU CCU AUU U-3' (2WJ), 5'-Cy5 GGC GUG GUA CAU UAC CUG GUA CGA GUU GAC-3' (3WJ/4WJ/4WJ single-loop (SL)), 5'GUC AAC UCG UUC GCdA GUC CUA UUU-3' (3WJ), 5'-GCA AGC CAC CUC GCdA GUC CUA UUU-3' (4WJ), 5'-GUC AAC UCG UGG UGG CUU GC-3' (4WJ/4WJ SL), 5'-Cy5 GGC GUG GUA CAU UAC CUG GUA CCC CCU CGC GAG CCU AUU U-3' (2WJ SL), 5' -GCA AGC CAC CUC GCG AGC CUA UUU-3' (4WJ SL) and 5'-Cy3 AAA UAG GCU CGC GAA CCA GAG AAA CAC ACG CC-3' (2WJ & 4WJ SL)
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