| Autor: |
Evstigneeva ZG; Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 117071 Russia., Solov'eva NA, Sidel'nikova LI |
| Jazyk: |
ruština |
| Zdroj: |
Prikladnaia biokhimiia i mikrobiologiia [Prikl Biokhim Mikrobiol] 2001 Jan-Feb; Vol. 37 (1), pp. 5-18. |
| Abstrakt: |
Folding and assembling of newly synthesized proteins is directed and effected by a group of relatively recently discovered proteins called molecular chaperones. These proteins not only control the assembling of native structures; they also remodel protein molecules that have wrong conformations. All molecular chaperones perform the same function, but structurally they are divided into groups of chaperones and chaperonins. These proteins are highly conserved in evolution and display an ATPase activity. Certain known chaperones and chaperonins are shown in the table, and their structures and mechanisms of action are described. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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