ライブラリ登録: Guest
Begell Digital Portal Begellデジタルライブラリー 電子書籍 ジャーナル 参考文献と会報 リサーチ集
International Journal for Multiscale Computational Engineering
インパクトファクター: 1.016 5年インパクトファクター: 1.194 SJR: 0.554 SNIP: 0.82 CiteScore™: 2

ISSN 印刷: 1543-1649
ISSN オンライン: 1940-4352

International Journal for Multiscale Computational Engineering

DOI: 10.1615/IntJMultCompEng.v7.i3.70
pages 237-250

Atomistically Informed Mesoscale Model of Alpha-Helical Protein Domains

Jeremie Bertaud
Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Zhao Qin
Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Markus J. Buehler
Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA

要約

Multiscale mechanical properties of biological protein materials have been the focal point of extensive investigations over the past decades. In this article, we present the development of a mesoscale model of alpha-helical (AH) protein domains, key constituents in a variety of biological materials, including cells, hair, hooves, and wool. Our model, derived solely from results of full atomistic simulations, is suitable to describe the deformation and fracture mechanics over multiple orders of magnitude in time- and length scales. After validation of the mesoscale model against atomistic simulation results, we present two case studies, in which we investigate, first, the effect of the length of an AH protein domain on its strength properties, and second, the effect of the length of two parallel AH protein domain arrangement on its shear strength properties and deformation mechanisms. We find that longer AHs feature a reduced tensile strength, whereas the tensile strength is maximized for ultrashort protein structures. Moreover, we find that the shearing of two parallel AHs engenders sliding, rather than AH unfolding, and that the shear strength does not significantly depend on the length of the two AHs.


Articles with similar content:

BACKSCATTER FROM A SCALE-SIMILARITY MODEL: EMBEDDED LES OF CHANNEL FLOW, DEVELOPING BOUNDARY LAYER FLOW AND BACKSTEP FLOW
TSFP DIGITAL LIBRARY ONLINE, Vol.8, 2013, issue
Lars Davidson
NONCIRCULAR CFRP BICYCLE'S CHAINRING, PART II: FINITE ELEMENT ANALYSIS
Composites: Mechanics, Computations, Applications: An International Journal, Vol.9, 2018, issue 3
Abdelrahman Elmikaty, Zhorachaid Thanawarothon, Christophe Bouvet, Laurent Mezeix
NONLINEAR BEHAVIOR OF MASONRY WALLS: FE, DE, AND FE/DE MODELS
Composites: Mechanics, Computations, Applications: An International Journal, Vol.10, 2019, issue 3
Daniele Baraldi, Emilio Meroi, Antonella Cecchi, Emanuele Reccia, Claudia Brito de Carvalho Bello
Brain Lipoprotein Metabolism and Its Relation to Neurodegenerative Disease
Critical Reviews™ in Neurobiology, Vol.13, 1999, issue 4
Marc Danik, Uwe Beffert, Danielle Champagne, Caroline Petit-Turcotte, Judes Poirier
MODELING OF THIN COMPOSITE LAMINATES WITH GENERAL ANISOTROPY UNDER HARMONIC VIBRATIONS BY THE ASYMPTOTIC HOMOGENIZATION METHOD
International Journal for Multiscale Computational Engineering, Vol.15, 2017, issue 3
I.D. Dimitrienko, Yu. I. Dimitrienko