Understanding anomalous mobility of proteins on SDS‐PAGE with special reference to the highly acidic extracellular domains of human E‐ and N‐cadherins-Reference-Cited by-同舟云学术

Understanding anomalous mobility of proteins on SDS‐PAGE with special reference to the highly acidic extracellular domains of human E‐ and N‐cadherins

Published:2019-02-12 Issue:9 Volume:40 Page:1273-1281
ISSN:0173-0835
Container-title:ELECTROPHORESIS
language:en
Short-container-title:ELECTROPHORESIS

Author:

Tiwari Prince¹,Kaila Pallavi¹,Guptasarma Purnananda¹^ORCID

Affiliation:

1. Centre for Protein ScienceDesign and EngineeringDepartment of Biological SciencesIndian Institute of Science Education and Research (IISER) Mohali Punjab India

Publisher

Wiley

Subject

Clinical Biochemistry,Biochemistry,Analytical Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/elps.201800219

Reference16 articles.

1. The Achilles’ Heel of “Ultrastable” Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in Proteins Carrying Overall Positive Charge

2. Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior

3. Anomalous electrophoretic behavior of a very acidic protein: Ribonuclease U2

4. An equation to estimate the difference between theoretically predicted and SDS PAGE-displayed molecular weights for an acidic peptide

5. Structure and Biochemistry of Cadherins and Catenins

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