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|Title:||Conformations of hydrophobic peptides in trifluoroethanol, water and in solid state: A circular dichroism and Fourier Transform Infrared study|
|Authors:||Jagannadham, Medicharala V|
Krishnamurthy, Akella S R
|Abstract:||The conformations of peptides corresponding to KLLIALVLCFLPLAALG have been examined in trifluoroethanol (TFE), aqueous medium by circular dichroism spectroscopy and in the solid state by Fourier Transform Infra Red Spectroscopy (FTIR). The l7-residue parent peptide and peptides corresponding to shorter segments LVLCFLPLAALG and CFLPLAALG showed preference for helical conformation in TFE. Even the shorter hydrophobic peptides corresponding to KLLIA and LVL showed propensity for β-turn conformations in TFE. However, peptides corresponding to the relatively polar segment FLPLAALG were unordered in TFE. In water, peptides that showed ordered conformation in TFE preferred β-conformation. In solid-state, FTIR spectra indicated that the hydrophobic peptides adopt β -structures with extensive hydrogen bond network in the solid state. The hydrophobic core segment thus appears to dictate the conformational propensity of the peptide.|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.36(6) [December 1999]|
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