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Noah E. Robinson
Proceedings of the National Academy of Sciences of the United States of America
Vol. 99, No. 8 (Apr. 16, 2002), pp. 5283-5288
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3058484
Page Count: 6
You can always find the topics here!Topics: Amides, Hydrogen bonds, Proteins, Atoms, Coefficients, Databases, Phosphates, Hydrogen, Estimation methods, Computer software
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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 experimental measurements. These rates demonstrate that deamidation may be a biologically relevant phenomenon in a remarkably large percentage of proteins.
Proceedings of the National Academy of Sciences of the United States of America © 2002 National Academy of Sciences