| Title: |
Thermal stability of the hemagglutinin‐neuraminidase from Sendai virus evidences two folding domains |
| Authors: |
Manfrinato, Maria Cristina; Bellini, Tiziana; Masserini, Massimo; Tomasi, Maurizio; Dallocchio, Franco |
| Source: |
FEBS Letters ; volume 495, issue 1-2, page 48-51 ; ISSN 0014-5793 1873-3468 |
| Publisher Information: |
Wiley |
| Publication Year: |
2001 |
| Collection: |
Wiley Online Library (Open Access Articles via Crossref) |
| Description: |
The domain structure of hemagglutinin‐neuraminidase from Sendai virus (cHN) was investigated by studying the thermal stability in the 20–100°C range. Differential scanning calorimetry evidences two conformational transitions. The first transition is apparently a reversible two‐state process, with T m 48.3°C, and is shifted to 50.1°C in the presence of the substrate analogue 2,3‐dehydro‐2‐deoxy‐ N ‐acetyl neuraminic acid, meaning that the substrate binding domain is involved in the transition. The second transition, with apparent T m 53.2°C, is accompanied by irreversible loss of enzymatic activity of the protein, and the presence of the substrate analogue does not affect the T m . The data indicate that cHN is composed of two independent folding domains, and that only one domain is involved in the binding of the substrate. Our results suggest that the paramyxovirus neuraminidases have the folding properties of a two‐domain protein. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1016/s0014-5793(01)02362-6 |
| DOI: |
10.1016/S0014-5793%2801%2902362-6 |
| Availability: |
http://dx.doi.org/10.1016/s0014-5793(01)02362-6; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2FS0014-5793%2801%2902362-6; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2FS0014-5793(01)02362-6; https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2801%2902362-6 |
| Rights: |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
| Accession Number: |
edsbas.366ECE63 |
| Database: |
BASE |