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Urea and Acid Induced Unfolding of Fatted and Defatted Human Serum Albumin

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Urea induced equilibrium unfolding of fatted and defatted human serum albumin (HSA) showed that fatty acid stabilizes native and intermediate states. Similarly acid induced unfolding of fatted and defatted HSA also showed that fatty acid stabilizes NF and FE transitions. These results also showed that five electrostatic interactions along with one buried carboxyl group of acidic amino acid are involved in acid induced unfolding of HSA.

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Keywords: Acid induced unfolding; conformational stability; hydrodynamic volume; intrinsic viscosity; urea induced unfolding

Document Type: Research Article

Publication date: 2008-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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