TY - JOUR
T1 - Biophysical characterization of an insect lysozyme from Manduca sexta
AU - López-Zavala, Alonso A.
AU - De-La-Re-Vega, Enrique
AU - Calderón-Arredondo, Sergio A.
AU - García-Orozco, Karina D.
AU - Velázquez, Enrique F.
AU - Islas-Osuna, Maria A.
AU - Valdez, Miguel A.
AU - Sotelo-Mundo, Rogerio R.
PY - 2004/2
Y1 - 2004/2
N2 - 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.
AB - 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.
KW - Circular dichroism
KW - Dynamic light scattering
KW - Insect
KW - Lysozyme
KW - Manduca sexta
KW - Secondary structure
UR - http://www.scopus.com/inward/record.url?scp=1542474005&partnerID=8YFLogxK
U2 - 10.2174/0929866043478374
DO - 10.2174/0929866043478374
M3 - Artículo
SN - 0929-8665
VL - 11
SP - 85
EP - 92
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
IS - 1
ER -