Dergi makalesi Açık Erişim

Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study

Avilov, SV; Aleksandrova, NA; Demchenko, AP


Citation Style Language JSON

{
  "URL": "https://aperta.ulakbim.gov.tr/record/93943", 
  "abstract": "The interactions between an oligomeric heat-shock protein, alpha-crystallin, and its individual subunits with unfolded proteins were monitored by surface plasmon resonance. Immobilization at the sensor chip allowed us for the first time to study isolated alpha-crystallin subunits under physiological conditions. We observe that these subunits, in contrast to alpha-crystallin oligomers, do not bind unfolded protein. Our data indicate that quaternary structure of alpha-crystallin is necessary for its chaperone-like activity.", 
  "author": [
    {
      "family": "Avilov", 
      "given": " SV"
    }, 
    {
      "family": "Aleksandrova", 
      "given": " NA"
    }, 
    {
      "family": "Demchenko", 
      "given": " AP"
    }
  ], 
  "container_title": "PROTEIN AND PEPTIDE LETTERS", 
  "id": "93943", 
  "issue": "1", 
  "issued": {
    "date-parts": [
      [
        2004, 
        1, 
        1
      ]
    ]
  }, 
  "page": "41-48", 
  "title": "Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study", 
  "type": "article-journal", 
  "volume": "11"
}
6
2
görüntülenme
indirilme
Görüntülenme 6
İndirme 2
Veri hacmi 444 Bytes
Tekil görüntülenme 6
Tekil indirme 2

Alıntı yap