English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The Y9P variant of the titin I27 module: Structural determinants of its revisited nanomechanics.

Oroz, J., Bruix, M., Laurents, D. V., Galera-Prat, A., Schönfelder, J., Canada, F. J., et al. (2016). The Y9P variant of the titin I27 module: Structural determinants of its revisited nanomechanics. Structure, 24(4), 606-616. doi:10.1016/j.str.2016.02.016.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5773-B Version Permalink: http://hdl.handle.net/21.11116/0000-0001-1C72-0
Genre: Journal Article

Files

show Files
hide Files
:
2281698.pdf (Publisher version), 3MB
 
File Permalink:
-
Name:
2281698.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2281698_Suppl_1.pdf (Supplementary material), 801KB
Name:
2281698_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2281698_Suppl_2.pdf (Supplementary material), 4MB
Name:
2281698_Suppl_2.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Oroz, J.1, Author              
Bruix, M., Author
Laurents, D. V., Author
Galera-Prat, A., Author
Schönfelder, J., Author
Canada, F. J., Author
Carrion-Vazquez, M., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: -
 Abstract: The titin I27 module from human cardiac titin has become a standard in protein nanomechanics. A proline-scanning study of its mechanical clamp found three mechanically hypomorphic mutants and a paradoxically hypermorphic mutant (I27Y9P). Both types of mutants have been commonly used as substrates of several protein unfoldase machineries in studies relating protein mechanostability to translocation or degradation rates. Using single-molecule force spectroscopy based on atomic force microscopy, polyprotein engineering, and steered molecular dynamics simulations, we show that, unexpectedly, the mechanostability of the Y9P variant is comparable to the wild type. Furthermore, the NMR analysis of homomeric polyproteins of this variant suggests that these constructs may induce slight structural perturbations in the monomer, which may explain some minor differences in this variant's properties; namely the abolishment of the mechanical unfolding intermediate and a reduced thermal stability. Our results clarify a previously reported paradoxical result in protein nanomechanics and contribute to refining our toolbox for understanding the unfolding mechanism used by translocases and degradation machines.

Details

show
hide
Language(s): eng - English
 Dates: 2016-03-242016-04-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2016.02.016
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 24 (4) Sequence Number: - Start / End Page: 606 - 616 Identifier: -