Secondary Structure of the Homologous Proteins, A A-Fetoprotein and Serum Albumin, from their Circular Dichroism and Infrared Spectra

Authors: Oberg K.A.; Uversky V.N.

Source: Protein and Peptide Letters, Volume 8, Number 4, August 2001 , pp. 297-302(6)

Publisher: Bentham Science Publishers

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Abstract:

Secondary structure composition of two homologous proteins, alpha-fetoprotein and serum albumin, has been compared using circular dichroism and Fourier-transform infrared spectroscopy. CD-only analysis gives an accurate a-helical content for SA, but underestimates the predicted value for AFP. In contrast, FTIR-only analysis underestimates the helical content of SA. However, analysis of hybrid IR-CD spectra gives more accurate values for secondary structure composition for both AFP and SA and shows that the secondary structures of these proteins are the same.

Keywords: Proteins Fetoprotein; Serum Albumin; Circular Dichroism; Human serum albumin (HSA)

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409391

Publication date: 2001-08-01

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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.