Binding studies of metal ions and dyes with biopolymers

The identification of the binding sites in the peptide chain and conformational changes as a consequence of the metal-protein interaction as well as the lability of this interaction can explain the role of these metal-based bio molecules in living organisms. Present work attempts to critically review methods for assessing the structure characterization of the metal binding sites as well as the class of proteins involved in some metal- binding proteins are discussed. Recent developments when assessing metallo-proteins and metal-protein complexes in the clinical environmental and food fields and pioneering research regarding nano- particle-protein characterization are also reviewed. The present book consists of the following - 1. Studies on the binding of Congo red with a collagen. 2. The effect of physico-chemical factors on interaction between divalent metal ions and albumin. 3. Physico-chemical studies on the binding of Hg(II) and molybdenum (VI) ions with ribonucleic acid. 4. A polarographic study on the binding of metal ions with albumin. 5. The pH and diffusion current measurements on the binding of metal ions with albumin.