HSP70 chaperone functions in stressed cells.

Nollen, E. A., 2000, s.n.. 153 p.

Research output: ThesisThesis fully internal (DIV)Academic

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In orrder to grow, divide, and to exert their specialized functions, our cells depend on a multitude of different proteins with specific roles in the cell. Proteins are characterized by the order of their building stones, the amino acids, the length of the amino acid chain, and the way this chain is folded into a three dimensional structure. This three-dimensional form determines the function of a protein. Proteins in their functional form are folded in such a way that the water repelling segments of the chains are not in contact with the surrounding aqueous environment in the cell. If these so-called hydrophobic domains would be exposed, they could, besides with hydrophobic domains within the same proteins, also non-functionally and irreversibly stick to hydrophobic domains of other proteins. These non-procluctive interactions could then lead to misfolding and inactivation of the proteins involved. ... Zie: Summary
Original languageEnglish
QualificationDoctor of Philosophy
  • Konings, Anthonius, Supervisor
  • Morimoto, Richard I., Supervisor, External person
Print ISBNs9036713145
Publication statusPublished - 2000


  • Proefschriften (vorm), Cellen (biologie), Stress, Eiwitten, klinische pathologie

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