Protein deamidation

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Protein deamidation.

A completely automatic computerized technique for the quantitative estimation of the deamidation rates of any protein for which the three-dimensional structure is known has been developed. Calculations of the specific deamidation rates of 170,014 asparaginyl residues in 13,335 proteins have been carried out. The calculated values have good quantitative reliability when compared with experimenta...

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Peptidoglutaminase Deamidation of Proteins and Protein Hydrolysates for Improved Food

The limited deamidating ability of peptidoglutaminase {PGase) toward intact food proteins (0-6% deamidation) can be significantly enhanced by prior protein hydrolysis and altering protein conformation by such means as moist heat. PGase deamidation increases protein solubility and improves emulsifying and other physical properties under mildly acidic conditions. A batch reactor method was develo...

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Deamidation of human erythrocyte protein 4.1: possible role in aging.

The human erythrocyte membrane protein 4.1 exists in two major electrophoretic forms: 4.1a (80 Kd) and 4.1b (78 Kd). Mass spectrometry and amino acid analysis of the proteolytic peptides derived from carboxyl-terminal regions of these proteins indicate that they differ by deamidation of two aspargine residues at positions 478 and 502. Electrophoretic analysis of carboxyl-terminal peptides has s...

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Asparagine deamidation and the role of higher order protein structure.

The 'protein world' exhibits additional complexity caused by post-translational modifications. One such process is nonenzymic deamidation of asparagine which is controlled partly by primary sequence, but also higher order protein structure. We have studied the deamidation of an N-terminal peptide in muscle glyceraldehyde 3-phosphate dehydrogenase to relate three-dimensional structure, proteolys...

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Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase.

Modification of calmodulin by protein carboxyl methyltransferase requires deamidation of one or more labile asparagine residues (Johnson, B.A., Freitag, N. E., and Aswad, D. W. (1985) J. Biol. Chem. 260, 10913-10916). We now show that deamidation results in the generation of two altered forms of calmodulin, designated A and B, which can be separated by electrophoresis under nondenaturing condit...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2002

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.082102799