Neutralizing Positive Charges at the Surface of a Protein Lowers Its Rate of Amide Hydrogen Exchange without Altering Its Structure or Increasing Its Thermostability-Reference-Cited by-同舟云学术

Neutralizing Positive Charges at the Surface of a Protein Lowers Its Rate of Amide Hydrogen Exchange without Altering Its Structure or Increasing Its Thermostability

Published:2010-11-19 Issue:49 Volume:132 Page:17411-17425
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Shaw Bryan F.¹,Arthanari Haribabu¹,Narovlyansky Max¹,Durazo Armando¹,Frueh Dominique P.¹,Pollastri Michael P.¹,Lee Andrew¹,Bilgicer Basar¹,Gygi Steven P.¹,Wagner Gerhard¹,Whitesides George M.¹

Affiliation:

1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States, Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76706, United States, Department of Biological Chemistry and Molecular Pharmacology and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, United States, Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90024, United States, Department of Chemistry...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9067035

Reference82 articles.

1. Evaluating Electrostatic Contributions to Binding with the Use of Protein Charge Ladders

2. Why Are Proteins Charged? Networks of Charge–Charge Interactions in Proteins Measured by Charge Ladders and Capillary Electrophoresis

3. Peracetylated Bovine Carbonic Anhydrase (BCA-Ac18) Is Kinetically More Stable than Native BCA to Sodium Dodecyl Sulfate

4. Measurement of Electrostatic Interactions in Protein Folding with the Use of Protein Charge Ladders

5. Increasing the Net Charge and Decreasing the Hydrophobicity of Bovine Carbonic Anhydrase Decreases the Rate of Denaturation with Sodium Dodecyl Sulfate

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