GroEL-induced stretching of a substrate protein: An EPR/SDSL study in BIOPHYSICAL JOURNAL, vol 88, issue 1, pp 562A-562A
2005 (English)In: BIOPHYSICAL JOURNAL, Elsevier (Cell Press) / Biophysical Society , 2005, Vol. 88, no 1, 562A-562A p.Conference paper (Refereed)
The Hsp60-type chaperonin GroEL assists in the folding of the enzyme Human Carbonic Anhydrase II (HCA II) and protects it from aggregation.It is still a controversy whether the action of GroEL is an active or passive process. Single- and double-cysteine mutants were specificallyspin labeled at a topological breakpoint in the β-core of HCA II. X-band electron paramagnetic resonance (EPR) was used at physiologicaltemperatures to monitor the GroEL-induced structural changes in this region of HCA II. Inter-residue distance calculations based on dipolarinteraction show that the proximity of the labeled positions F147 and K213 in the native state of HCA II is ~11±2 Å, and that it is virtuallyintact in the thermally-induced molten-globule state that binds to GroEL. However, upon interaction with GroEL a spin-spin distance increaseto ~22±3 Å indicates a conformational change in HCA II that is part of the GroEL-induced substrate stretch that enables structural rearrangementof a misfolded substrate protein.
Place, publisher, year, edition, pages
Elsevier (Cell Press) / Biophysical Society , 2005. Vol. 88, no 1, 562A-562A p.
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-75802ISI: 000226378502751OAI: oai:DiVA.org:liu-75802DiVA: diva2:509103
48th Rocky Mountain Conference on Analytical Chemistry, July 23-26, Breckenridge, USA