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Salt and pH-dependent properties of native and mutant insulin

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Chinese Science Bulletin

Abstract

A fast and effective model for predicting the salt and pH dependent properties of protein complexes is presented. It is based on the formal charge parameter sets of ionizable groups and applied in conjunction with the finite difference Poisson-Boltzmann (FDPB) method to calculate the electrostatic interactions. All simulations were performed on the native 2Zn insulin and its fast-acting mutants such as B9D (B9Ser→Asp), B9E (B9Aer→Glu), B9EB10D (B9Ser→ Glu, B10His→Asp), and B10D (B10His→Asp). The salt and pH dependent properties of these dimers were analyzed from the aspect of electrostatic interaction, and the theoretical basis of the fast-acting behavior of these mutants was explained. It is found that the results agree well with experimental observations.

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Authors and Affiliations

  1. Center for Biomedical Engineering, Beijing Polytechnic University, 100022, Beijing, China

    Xiaohui Ma, Chunhua Li, Benzhuo Lu, Weizu Chen & Cunxin Wang

  2. Department of Astronomy and Applied Physics, University of Science and Technology of China, 230026, Hefei, China

    Benzhuo Lu

  3. College of Chemistry & Molecular Engineering, Peking University, 100871, Beijing, China

    Xiaojie Xu

Authors
  1. Xiaohui Ma
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  2. Chunhua Li
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  3. Benzhuo Lu
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  4. Weizu Chen
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  5. Cunxin Wang
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  6. Xiaojie Xu
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Corresponding author

Correspondence to Cunxin Wang.

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Ma, X., Li, C., Lu, B. et al. Salt and pH-dependent properties of native and mutant insulin. Chin.Sci.Bull. 47, 464–466 (2002). https://doi.org/10.1360/02tb9107

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  • DOI: https://doi.org/10.1360/02tb9107

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