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Page Fig. III. 40 Scanning Electron Micrographs of (a) 15% and (b) 20% TTEGDA- crosslinked poly (acrylamide) s. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page Fig. III. 41. Scanning Electron Micrographs of (a) linear poly (acrylamide) and (b) 5% TTEGDA crossliked poly (acrylamide). (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page d. Effect of addition of a third component: terpolymerisation and subsequent morphology. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page Fig. III. 42. Scanning Electron Micrographs of (a) 10% DVB- crosslinked acrylamide-dimethylacrylamide terpolymer and (b) acrylamide copolymer. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page Fig. III. 43 Scanning Electron Micrographs of 10% NNMBA crosslinked acrylamide prepared (a) in bulk and (b) in film form. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page Fig. III. 44. (a,b) Scanning Electron Micrographs of 10% TTEGDA- crosslinked poly (acrylamide) in film form. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page Fig. III. 45. Scanning Electron Micrographs of 10% TTEGDA- crosslinked poly (acrylamide) after functionalisation with ethylenediamine. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page Fig. III. 46. (a,b) Scanning Electron micrographs of 2% TEGDMA- crosslinked poly (styrene) beads. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page a. Effect of nature of crosslinking. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page b. Effect of polymerisation conditions. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page c. Effect of addition of a third component. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page 5. Synthesis of crabrolin: Phe-Leu-Pro-Leu-Ile Leu-Arg-Lys-Ile-Val-Thr-Ala-Leu -a peptide toxin. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page 9. Attempt to attach the first amino acid as its acid chloride. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994
Page 11. cross linked terpolymers of acrylamide and N, N-dimethylacrylamide as supports. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis Mathew C Chandy Chemistry 1994
Page b. Deprotection and cleavage. (Thesis: Role of hydrophilicity-hydrophobicity balance of the polymeric supports in solid phase Peptide synthesis ) Mathew C Chandy Chemistry 1994



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