Structure analysis of collagen fibril at atomic-level resolution and its implications for intra-fibrillar transport in bone biomineralization-Reference-Cited by-同舟云学术

Structure analysis of collagen fibril at atomic-level resolution and its implications for intra-fibrillar transport in bone biomineralization

Published:2018 Issue:3 Volume:20 Page:1513-1523
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Xu Zhijun¹²³⁴⁵^ORCID,Zhao Weilong⁶⁷⁸⁹^ORCID,Wang Ziqiu⁶⁷⁸⁹,Yang Yang¹⁰¹¹¹²⁹¹³,Sahai Nita⁶⁷⁸⁹¹⁴^ORCID

Affiliation:

1. State Key Laboratory of Materials-Oriented Chemical Engineering

2. College of Chemical Engineering

3. Nanjing Tech University

4. Nanjing 210009

5. China

6. Department of Polymer Science

7. University of Akron

8. Akron

9. USA

10. Department of Chemistry and Biochemistry

11. Rowan University

12. Glassboro

13. Department of Chemistry

14. Integrated Bioscience Program

Abstract

A comprehensive all-atom structural analysis of Tye I collagen fibril reveals that a uniform sub-channel with preferred orientation of charged amino acid sidechains into hole zones exists only at the a1–a3 bands, which coincide with the earliest mineralization locations.

Funder

University of Akron

National Natural Science Foundation of China

Natural Science Foundation of Jiangsu Province

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP05261H

Reference55 articles.

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5. Molecular Models Illustrating the Possible Distributions of ‘Holes’ in Simple Systematically Staggered Arrays of Type I Collagen Molecules in Native-Type Fibrils

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