Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy (Articolo in rivista)

Type
Label
  • Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1046/j.1365-2818.2001.00891.x (literal)
Alternative label
  • Valle, F; Derose, JA; Dietler, G; Kawe, M; Pluckthun, A; Semenza, G (2001)
    Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy
    in Journal of microscopy (Print); Blackwell Scientific Publications, Oxford (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Valle, F; Derose, JA; Dietler, G; Kawe, M; Pluckthun, A; Semenza, G (literal)
Pagina inizio
  • 195 (literal)
Pagina fine
  • 198 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 203 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 4 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [ 1 ] Univ Lausanne, Inst Phys Mat Condensee, BSP, CH-1015 Lausanne, Switzerland [ 2 ] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland [ 3 ] ETH Zentrum, Swiss Fed Inst Technol, Inst Biochem, CH-8092 Zurich, Switzerland [ 4 ] Univ Milan, Inst Biochim, I-20133 Milan, Italy (literal)
Titolo
  • Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy (literal)
Abstract
  • Most sample preparation methods for scanning probe or electron microscopy require that biomolecules, such as proteins, be fixed. Fixation destroys the molecular functionality and can possibly affect the true molecular structure. Here we report sample preparation conditions that allow the imaging of an unfixed protein, GroEL, under in-vivo conditions. by atomic force microscopy. Under these conditions, the protein should maintain its native structure and biological activity. The typical toroidal shape with pore of the GroEL complex was easily visible in the images. Images of a single complex show dimensions that agree well with crystallographic data. Under in-vivo conditions. it should be possible to study the biological activity and function of proteins (literal)
Editore
Prodotto di
Autore CNR

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Editore di
data.CNR.it