Hierarchical chemo-nanomechanics of proteins: entropic elasticity, protein unfolding and molecular fracture

Buehler, Markus J.

doi:10.2140/jomms.2007.2.1019

Cited by 28 publications

(19 citation statements)

References 82 publications

(129 reference statements)

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“…This behavior is similar to those observed in experimental studies [30,31]. It is noted that the plateau regime is followed by a steep increase in the force-extension relation once the backbone covalent bonds are being stretched, upon complete uncoiling of the AH structure [32,33] (this behavior is not explicitly shown in Fig. 3(a) as we the atomistic model and computational approach, we refer the reader to the original publications [26,27] (here we provide only a brief review of the most important aspects).…”

Section: Nano Researchsupporting

confidence: 88%

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Elasticity, strength and resilience: A comparative study on mechanical signatures of α-Helix, β-sheet and tropocollagen domains

Buehler

Keten

2008

Nano Res.

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In biology, structural design and materials engineering is unified through formation of hierarchical features with atomic resolution, from nano to macro. Three molecular building blocks are particularly prevalent in all structural protein materials: alpha helices (AHs), beta-sheets (BSs) and tropocollagen (TC). In this article we present a comparative study of these three key building blocks by focusing on their mechanical signatures, based on results from full-atomistic simulation studies. We fi nd that each of the basic structures is associated with a characteristic material behavior: AH protein domains provide resilience at large deformation through energy dissipation at low force levels, BS protein domains provide great strength under shear loading, and tropocollagen molecules provide large elasticity for deformation recovery. This suggests that AHs, BSs, and TC molecules have mutually exclusive mechanical signatures. We correlate each of these basic properties with the molecule's structure and the associated fundamental rupture mechanisms. Our study may enable the use of abundant protein building blocks in nanoengineered materials, and may provide critical insight into basic biological mechanisms for bio-inspired nanotechnologies. The transfer towards the design of novel nanostructures could lead to new multifunctional and mechanically active, tunable, and changeable materials.

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Section: Nano Researchsupporting

confidence: 88%

“…Rupture of the AH structure after stretching the covalent backbone occurs at force levels of 5 7 nN [32].…”

Section: Comparative Analysismentioning

confidence: 99%

Elasticity, strength and resilience: A comparative study on mechanical signatures of α-Helix, β-sheet and tropocollagen domains

Buehler

Keten

2008

Nano Res.

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“…Email: wwlu@hku.hk Color versions of one or more of the figures in the article can be found online at www.tandfonline.com/lsfm. I rather than type II collagen fibrils from AC (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Recently, the nanomechanical properties of AC collagen fibrils were examined in various animal models and human OA specimens via atomic force microscopy (AFM) nanoindentation (18)(19)(20).…”

Section: Introductionmentioning

confidence: 99%

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

et al. 2014

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Osteoarthritis (OA) is a prevalent and deliberating joint disorder, which acts as the leading cause for the disability and poor quality of life of the middle-age and elderly people. It is generally believed that OA is degeneration of articular cartilage. However, the debate remains on the role of subchondral bone in pathogenesis of OA. In this study, the nanostiffness of collagen fibrils from articular cartilage in patients with entirely different bone metabolism, that is, OA, osteoporosis (OP), and health, was quantitatively measured with AFM nanoindentation technique. It was found that the stiffness of individual collagen fibril from healthy cartilage was 2.67 ± 0.12GPa under ambient condition and 11.24 ± 0.74MPa in hydrated state respectively. The collagen fibrils were softer in osteoporosis (OP) group (ambient: 1.64 ± 0.12GPa; hydrated: 8.59 ± 0.59MPa). By contrast, the extracted fibrils from OA cartilages were stiffer (ambient: 4.65 ± 0.25GPa; hydrated: 17.26 ± 1.77MPa). The results obtained demonstrated that the collagen fibrils extracted from OA patients are stiffer than those from healthy patients, and therefore the nanomechanical characterization of extracted collagen fibrils may be a promising way for early diagnosis of OA.

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“…For failure properties of materials ͑which naturally involves large bond deformation and bond rupture mechanisms͒, this translates into the properties of molecules at large strain, a phenomenon also referred to as hyperelasticity. Strachan et al, 2003Strachan et al, , 2005van Duin et al, 2004;Chenoweth et al, 2005;Han et al, 2005;Nielson et al, 2005;Buehler, 2007b;Buehler et al, 2007͒. To describe the details of bond stretching and breaking, a bond length-bond order relationship is employed to obtain smooth transition from nonbonded to single, double, and triple bonded systems. All connectivity-dependent interactions ͑that means valence and torsion angles͒ are formulated to be bond-order dependent.…”

Section: A Conventional and Reactive Force Fieldsmentioning

confidence: 99%

Colloquium: Failure of molecules, bones, and the Earth itself

Buehler

Keten

2010

Rev. Mod. Phys.

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Materials fail by recurring rupture and shearing of interatomic bonds at microscopic, molecular scales, leading to disintegration of matter at macroscale and a loss of function. In this Colloquium, the state-of-the-art of investigations on failure mechanisms in materials are reviewed, in particular focusing on atomistic origin of deformation and fracture and relationships between molecular mechanics and macroscale behavior. Simple examples of fracture phenomena are used to illustrate the significance and impact of material failure on our daily lives. Based on case studies, mechanisms of failure of a wide range of materials are discussed, ranging from tectonic plates to rupture of single molecules, and an explanation on how atomistic simulation can be used to complement experimental studies and theory to provide a novel viewpoint in the analysis of complex systems is provided. Biological protein materials are used to illustrate how extraordinary properties are achieved through the utilization of intricate structures where the interplay of weak and strong chemical bonds, size and confinement effects, and hierarchical features play a fundamental role. This leads to a discussion of how even the most robust biological material systems fail, leading to diseases that arise from structural and mechanical alterations at molecular, cellular, and tissue levels. New research directions in the field of materials failure and materials science are discussed and the impact of improving the current understanding of materials failure for applications in nanotechnology, biotechnology, medicine as well as the built environment.

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Hierarchical chemo-nanomechanics of proteins: entropic elasticity, protein unfolding and molecular fracture

Cited by 28 publications

References 82 publications

Elasticity, strength and resilience: A comparative study on mechanical signatures of α-Helix, β-sheet and tropocollagen domains

Elasticity, strength and resilience: A comparative study on mechanical signatures of α-Helix, β-sheet and tropocollagen domains

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

Colloquium: Failure of molecules, bones, and the Earth itself

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