English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Shifting transition states in the unfolding of a large ankyrin repeat protein

Werbeck, N. D., Rowling, P. J. E., Chellamuthu, V. R., & Itzhaki, L. S. (2008). Shifting transition states in the unfolding of a large ankyrin repeat protein. Proceedings of the National Academy of Sciences of the United States of America (Astor), 105(29), 9982-9987. doi:10.1073/pnas.0705300105.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-A64E-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-DEEB-E
Genre: Journal Article

Files

show Files
hide Files
:
PNAS_105_2008_9982.pdf (Any fulltext), 731KB
 
File Permalink:
-
Name:
PNAS_105_2008_9982.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Werbeck, Nicolas D.1, Author              
Rowling, Pamela J. E., Author
Chellamuthu, Vasuki R., Author
Itzhaki, Laura S., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: The 33-amino-acid ankyrin motif comprises a β-turn followed by two anti-parallel α-helices and a loop and tandem arrays of the motif pack in a linear fashion to produce elongated structures characterized by short-range interactions. In this article we use site-directed mutagenesis to investigate the kinetic unfolding mechanism of D34, a 426-residue, 12-ankyrin repeat fragment of the protein ankyrinR. The data are consistent with a model in which the N-terminal half of the protein unfolds first by unraveling progressively from the start of the polypeptide chain to form an intermediate; in the next step, the C-terminal half of the protein unfolds via two pathways whose transition states have either the early or the late C-terminal ankyrin repeats folded. We conclude that the two halves of the protein unfold by different mechanisms because the N-terminal moiety folds and unfolds in the context of a folded C-terminal moiety, which therefore acts as a “seed” and confers a unique directionality on the process, whereas the C-terminal moiety folds and unfolds in the context of an unfolded N-terminal moiety and therefore behaves like a single-domain ankyrin repeat protein, having a high degree of symmetry and consequently more than one unfolding pathway accessible to it.

Details

show
hide
Language(s): eng - English
 Dates: 2007-06-062008-05-062008-07-162008-07-22
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America (Astor)
  Other : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 105 (29) Sequence Number: - Start / End Page: 9982 - 9987 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230