English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Role of Sacrificial Protein−Metal Bond Exchange in Mussel Byssal Thread Self-Healing

Schmitt, C. N. Z., Politi, Y., Reinecke, A., & Harrington, M. J. (2015). Role of Sacrificial Protein−Metal Bond Exchange in Mussel Byssal Thread Self-Healing. Biomacromolecules, 16(9), 2852-2861. doi:10.1021/acs.biomac.5b00803.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4B40-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-1D7C-5
Genre: Journal Article

Files

show Files
hide Files
:
2182698.pdf (Publisher version), 6MB
 
File Permalink:
-
Name:
2182698.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute of Colloids and Interfaces, MTKG; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2182698_supp.pdf (Supplementary material), 448KB
Name:
2182698_supp.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Schmitt, Clemens N. Z.1, Author              
Politi, Yael2, Author              
Reinecke, Antje1, Author              
Harrington, Matthew J.1, Author              
Affiliations:
1Matthew Harrington, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863292              
2Yael Politi, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863297              

Content

show
hide
Free keywords: -
 Abstract: Marine mussels tether to seashore surfaces with byssal threads ? proteinaceous fibers that effectively dissipate energy from crashing waves. Protein-metal coordination bonds have been proposed to contribute to the characteristic mechanical and self-healing properties of byssal threads; however, very little is understood about how these cross-links function at the molecular level. In the present study, combined Raman and X-ray absorption spectroscopy (XAS) measurements were employed to confirm the presence of protein-Zn2+ coordination bonds in the mussel byssus and to monitor transitions in the coordination structure during thread deformation and self-healing. Results indicate that Zn2+ coordination bonds, primarily mediated via histidine, are ruptured during thread yield and reformed immediately following thread relaxation. Mechanical healing, on the other hand, is correlated with the transition towards shorter coordination bond lengths. Calculation of the healing activation energy suggests that protein-Zn bond exchange provides a primary rate-limiting step during healing.

Details

show
hide
Language(s):
 Dates: 2015-08-212015
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1021/acs.biomac.5b00803
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 16 (9) Sequence Number: - Start / End Page: 2852 - 2861 Identifier: ISSN: 1525-7797
CoNE: https://pure.mpg.de/cone/journals/resource/969870273004