Protein folding pathways determined using disuplhide bonds
Article Abstract:
A number of investigators have questioned the disulphide bond formation process leading to the tertiary structure of bovine pancreatic trypsin inhibitor. According to J.S.Weisman and P.S. Kim, an intermediate containing a native disulphide bond (30-51) forms non-native 5-14 and 5-38 disulphides then forms a (30-51, 14-38) intermediate that is trapped with increasing concentrations of iodacetamide and iodoacetate. The same effect is also seen with acidifying agents, but less non-native disulphides are trapped given the same concentration.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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Complementation in beta-galactosidase: from protein structure to genetic engineering
Article Abstract:
Studies on beta-galactosidase enzymes showed that it exhibits alpha, omega and beta complementations. Compared to wild-types, these complemented enzymes only minimally recovered their activity after renaturation suggesting the absence of the connecting part of their polypeptides. With guanidine denaturation, full recovery of the peptides occured after removal of guanidine. An alpha and a 40 kildodalton omega peptide are essential for these observed effects.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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The evolution of molecular genetic pathways and networks
Article Abstract:
The influence of genetic pathway and network structures on the action of evolutionary forces is discussed. The relationships between network organization, topological architecture and evolutionary dynamics are investigated.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 2004
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