Biophysical characterization of an insect lysozyme from Manduca sexta

被引：3
|
作者：
López-Zavala, AA
de-la-Re-Vega, E
Calderón-Arredondo, SA
García-Orozco, KD
Velázquez, EF
Islas-Osuna, MA
Valdez, MA
Sotelo-Mundo, RR
机构：
[1] Sonoma State Univ, Poly & Mat Dept, Hermosillo, Sonora, Mexico
[2] Sonoma State Univ, Dept Phys, Hermosillo, Sonora, Mexico
[3] Sonoma State Univ, Aquaculture Grad Program, Hermosillo, Sonora, Mexico
来源：
PROTEIN AND PEPTIDE LETTERS | 2004年 / 11卷 / 01期
关键词：
lysozyme; insect; Manduca sexta; circular dichroisin; dynamic light scattering; secondary structure;
D O I：
10.2174/0929866043478374
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：85 / 92
页数：8
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