The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge

The effects of lacking a specific disulfide bridge on the transition state in folding were examined in order to explore the folding-unfolding mechanism of lysozyme. Four species of three-disulfide variant of hen lysozyme (3SS-lysozyme) were prepared by replacing two Cys residues with Ala or Ser: C6S...

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Vydáno v:	Journal of molecular biology Ročník 295; číslo 5; s. 1275 - 1288
Hlavní autoři:	Yokota, Atsushi, Izutani, Kazuki, Takai, Masanori, Kubo, Yukiko, Noda, Yasuo, Koumoto, Yasuko, Tachibana, Hideki, Segawa, Shin-ichi
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	England Elsevier Ltd 04.02.2000
Témata:	Amino Acid Substitution - genetics Animals Binding Sites Calorimetry Chickens Circular Dichroism Cysteine - genetics Cysteine - metabolism disulfide bridge Disulfides - metabolism Enzyme Stability Female Fluorescence Genetic Variation - genetics Guanidine - pharmacology Kinetics lysozyme variants Methionine - genetics Methionine - metabolism Models, Molecular Muramidase - chemistry Muramidase - genetics Muramidase - metabolism Protein Denaturation - drug effects protein engineering Protein Folding Protein Renaturation Protein Structure, Tertiary - drug effects Recombinant Proteins - chemistry Recombinant Proteins - metabolism Thermodynamics Titrimetry transition state Trisaccharides - metabolism triNAG CD lysozyme variants transition state HOHAHA SS1 protein engineering SS3 wtLYZ SS2 metLYZ SS4 DSC disulfide bridge ITC protein folding GuHCl 3SS-lysozyme rcmLYZ
ISSN:	0022-2836, 1089-8638
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