Cargando…
Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families
BACKGROUND: Disulphide bridges are well known to play key roles in stability, folding and functions of proteins. Introduction or deletion of disulphides by site-directed mutagenesis have produced varying effects on stability and folding depending upon the protein and location of disulphide in the 3-...
Autores principales: | Thangudu, Ratna R, Manoharan, Malini, Srinivasan, N, Cadet, Frédéric, Sowdhamini, R, Offmann, Bernard |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2628669/ https://www.ncbi.nlm.nih.gov/pubmed/19111067 http://dx.doi.org/10.1186/1472-6807-8-55 |
Ejemplares similares
-
Association of Putative Members to Family of Mosquito Odorant Binding Proteins: Scoring Scheme Using Fuzzy Functional Templates and Cys Residue Positions
por: Manoharan, Malini, et al.
Publicado: (2013) -
DSDBASE 2.0: updated version of DiSulphide dataBASE, a database on disulphide bonds in proteins
por: Kalmankar, Neha V, et al.
Publicado: (2022) -
Specialized structural and functional roles of residues selectively conserved in subfamilies of the pleckstrin homology domain family
por: Naveenkumar, Nagarajan, et al.
Publicado: (2019) -
Systematic search for putative new domain families in Mycoplasma gallisepticum genome
por: Reddy, Chilamakuri CS, et al.
Publicado: (2010) -
CUSP: an algorithm to distinguish structurally conserved and unconserved regions in protein domain alignments and its application in the study of large length variations
por: Sandhya, Sankaran, et al.
Publicado: (2008)