Solution conformation of poly(L-lysyl-L-glutamic acid) and poly(L-lysyl-L-glutamine)

Chauhan, V. S. ; Rao, M. V. R. ; Atreyi, M. ; Kumar, Satish (1984) Solution conformation of poly(L-lysyl-L-glutamic acid) and poly(L-lysyl-L-glutamine) International Journal of Peptide & Protein Research, 24 (1). pp. 48-54. ISSN 0367-8377

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1984.tb00926.x

Abstract

Solution conformation of poly(L-lysyl-L-glutamic acid) (PLGU) and poly(L-lysyl-L-glutamine) (PLGN) was studied in water as a function of pH, added salt, detergents, methanol and trifluoroethanol (TFE). Both the polypeptides exhibit no ordered conformation in the pH range 1.5-12.5; salts and detergents did not have any marked effect. Replacement of side chain carboxyl by an amide group did not help in inducing PLGN to adopt a helical conformation even at pH as high as 12.0, unlike poly(L-lysine). The helicogenic solvents, methanol and TFE, induce formation of weak helices in PLGU as well as in PLGN. It is not unlikely that H-bonding between the side chains leads to stabilizing an unordered conformations.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Amphoteric Polypeptide; Conformation; Glutaminyl Polypeptide; Glutamyl Polypeptide; Ionogenic Polypeptide; Lysyl Polypeptide; Polypeptide
ID Code:8179
Deposited On:26 Oct 2010 12:13
Last Modified:30 May 2011 11:52

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