Eight induced proteins were identified as DnaK protein, fabG4 protein, DNA-binding protein, hypothetical protein, two 14 kDa antigen and two 10 kDa chaperonin.
Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures.
Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant.
In an effort to examine the location and the conformational properties of a polypeptide chain substrate chaperonin
complexes, SANS experiments with contrast variation were undertaken at the NCNR by CARB (Center for Advanced Research in Biotechnology) and NCNR scientists, using a 86 % deuterated nonnative.
Although scientists have known for almost a decade that chaperonins aid proteins in folding, the precise mechanism of this process has remained murky.
Scientists had already generated precise pictures of chaperonins before and after these molecular guardians assisted in protein folding, but they lacked detailed images of what happens in between.
The universally conserved GroE (Hsp60) chaperonins
RUSSELL DOOLITTLE: Andrew (Roger), why do these organisms retain their chaperonins now that their mitochondria are gone?
A mitochondrial-like chaperonin 60 gene in Giardia lamblia: evidence that diplomonads once harbored an endosymbiont related to the progenitor of mitochondria.
Sigler and his colleagues looked at molecules called chaperonins, which help proteins fold into their final shapes.
These portals extend deep into the slice and probably provide the chaperonin with a place for processing energy-transfer molecules called ATP, Sigler notes.
play a natural role in reshaping mutant proteins and in keeping newly made proteins from tangling.