PUBLICATION

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

Authors
Guan, Y., Zhu, Q., Huang, D., Zhao, S., Jan Lo, L., Peng, J.
ID
ZDB-PUB-150828-3
Date
2015
Source
Scientific Reports   5: 13370 (Journal)
Registered Authors
Peng, Jinrong
Keywords
none
MeSH Terms
  • Acids/chemistry*
  • Amino Acid Sequence
  • Animals
  • Electrophoresis, Polyacrylamide Gel*
  • Glycosylation
  • Models, Chemical*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptides/chemistry*
  • Sumoylation
  • Ubiquitination
  • Zebrafish
  • Zebrafish Proteins/chemistry
PubMed
26311515 Full text @ Sci. Rep.
Abstract
The molecular weight (MW) of a protein can be predicted based on its amino acids (AA) composition. However, in many cases a non-chemically modified protein shows an SDS PAGE-displayed MW larger than its predicted size. Some reports linked this fact to high content of acidic AA in the protein. However, the exact relationship between the acidic AA composition and the SDS PAGE-displayed MW is not established. Zebrafish nucleolar protein Def is composed of 753 AA and shows an SDS PAGE-displayed MW approximately 13 kDa larger than its predicted MW. The first 188 AA in Def is defined by a glutamate-rich region containing ~35.6% of acidic AA. In this report, we analyzed the relationship between the SDS PAGE-displayed MW of thirteen peptides derived from Def and the AA composition in each peptide. We found that the difference between the predicted and SDS PAGE-displayed MW showed a linear correlation with the percentage of acidic AA that fits the equation y = 276.5x - 31.33 (x represents the percentage of acidic AA, 11.4% ≤ x ≤ 51.1%; y represents the average ΔMW per AA). We demonstrated that this equation could be applied to predict the SDS PAGE-displayed MW for thirteen different natural acidic proteins.
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Human Disease / Model
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