Alleviation of a defect in protein folding by increasing the rate of subunit assembly.

@article{Aramli2001AlleviationOA,
  title={Alleviation of a defect in protein folding by increasing the rate of subunit assembly.},
  author={Lili A. Aramli and Carolyn M Teschke},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 27},
  pages={25372-7}
}
Understanding the nature of protein grammar is critical because amino acid substitutions in some proteins cause misfolding and aggregation of the mutant protein resulting in a disease state. Amino acid substitutions in phage P22 coat protein, known as tsf (temperature-sensitive folding) mutations, cause folding defects that result in aggregation at high temperatures. We have isolated global su (suppressor) amino acid substitutions that alleviate the tsf phenotype in coat protein (Aramli, L. A… CONTINUE READING

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Electrophoresis: Theory, Techniques and Biochemical and Clinical Application

  • A. T. Andrews
  • 1986

hp://w w w .jb.org/ D

  • D. P. Goldenberg, D. H. Smith, J. King
  • Proc. Natl. Acad. Sci. USA
  • 1983

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