Biophysical characterization of an insect lysozyme from Manduca sexta

Alonso A. López-Zavala, Enrique De-La-Re-Vega, Sergio A. Calderón-Arredondo, Karina D. García-Orozco, Enrique F. Velázquez, Maria A. Islas-Osuna, Miguel A. Valdez, Rogerio R. Sotelo-Mundo*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Insect lysozyme from Manduca sexta (MS-lys) was overexpressed in E. coli and refolded to obtain active protein. Recombinant MS-lys presented a globular structure, with an alpha-helical content of 57% as assessed by circular dichroism spectroscopy. Light scattering studies showed that in solution MS-lys has a quasi-monodisperse size distribution, with a rod-like structure similar to nucleation clusters reported in egg lysozyme pre-crystallization stages. These results show that MS-lys is an excellent candidate for crystallization, folding and denaturation studies.

Original languageEnglish
Pages (from-to)85-92
Number of pages8
JournalProtein and Peptide Letters
Issue number1
StatePublished - Feb 2004


  • Circular dichroism
  • Dynamic light scattering
  • Insect
  • Lysozyme
  • Manduca sexta
  • Secondary structure


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