Cargando…
"Hot cores" in proteins: Comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms
BACKGROUND: A wide variety of stabilizing factors have been invoked so far to elucidate the structural basis of protein thermostability. These include, amongst the others, a higher number of ion-pairs interactions and hydrogen bonds, together with a better packing of hydrophobic residues. It has bee...
Autores principales: | Paiardini, Alessandro, Sali, Riccardo, Bossa, Francesco, Pascarella, Stefano |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2294123/ https://www.ncbi.nlm.nih.gov/pubmed/18312638 http://dx.doi.org/10.1186/1472-6807-8-14 |
Ejemplares similares
-
Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase
por: Liu, Liangwei, et al.
Publicado: (2012) -
Stability of the ‘L12 stalk’ in ribosomes from mesophilic and (hyper)thermophilic Archaea and Bacteria
por: Shcherbakov, D., et al.
Publicado: (2006) -
Discrimination of thermophilic and mesophilic proteins
por: Taylor, Todd J, et al.
Publicado: (2010) -
CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology
por: Paiardini, Alessandro, et al.
Publicado: (2005) -
PyMod: sequence similarity searches, multiple sequence-structure alignments, and homology modeling within PyMOL
por: Bramucci, Emanuele, et al.
Publicado: (2012)