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

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

(2016) Javed M. Khan et al.   BIOCHEMISTRY

Creation of active TIM barrel enzymes through genetic fusion of half-barrel domain constructs derived from two distantly related glycosyl hydrolases

(2016) Prerna Sharma et al.   FEBS Journal

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

(2015) Yihong Guan et al.   Scientific Reports

Hyperthermophile Protein Behavior: Partially-Structured Conformations of Pyrococcus furiosus Rubredoxin Monomers Generated through Forced Cold-Denaturation and Refolding

(2014) Sanjeev Kumar Chandrayan et al.   PLoS One

SDS Can Be Utilized as an Amyloid Inducer: A Case Study on Diverse Proteins

(2012) Javed Masood Khan et al.   PLoS One

Finding one's way in proteomics: a protein species nomenclature

(2009) Hartmut Schlüter et al.   Chemistry Central Journal

Structure and Biochemistry of Cadherins and Catenins

(2009) L. Shapiro et al.   Cold Spring Harbor Perspectives in Biology

The speciation of the proteome

(2008) Peter R Jungblut et al.   Chemistry Central Journal

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein

(2008) Sanjeev Kumar Chandrayan et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS