Cargando…
Helicity propensity and interaction of synthetic peptides from heptad-repeat domains of herpes simplex virus 1 glycoprotein H: A circular dichroism study
The secondary structure of two synthetic peptides from heptad-repeat domains of herpes simplex virus 1 glycoprotein H was determined by circular dichroism. In particular, the propensity of these peptides to assume an ordered structure was investigated upon by changing the solvent's polarity and...
Autores principales: | Sanavio, Barbara, Piccoli, Angela, Gianni, Tatiana, Bertucci, Carlo |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185525/ https://www.ncbi.nlm.nih.gov/pubmed/17560181 http://dx.doi.org/10.1016/j.bbapap.2007.04.019 |
Ejemplares similares
-
Heptad-repeat sequences in the glycoprotein of rhabdoviruses
por: Morales Coll, Julio
Publicado: (1995) -
Formation of functional super-helical assemblies by constrained single heptad repeat
por: Mondal, Sudipta, et al.
Publicado: (2015) -
SARS-CoV heptad repeat 2 is a trimer of parallel helices
por: Celigoy, Jessica, et al.
Publicado: (2011) -
Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region
por: Follis, Kathryn E., et al.
Publicado: (2005) -
Precise detection of circular dichroism in a cluster of nano-helices by photoacoustic measurements
por: Benedetti, Alessio, et al.
Publicado: (2017)