Abstract
AbstractProteins constitute the elementary building blocks of a vast variety of biological materials such as cellular protein networks, spider silk or bone, where they create extremely robust, multi-functional materials by self-organization of structures over many length- and time scales, from nano to macro. Some of the structural features are commonly found in a many different tissues, that is, they are highly conserved. Examples of such universal building blocks include alpha-helices, beta-sheets or tropocollagen molecules. In contrast, other features are highly specific to tissue types, such as particular filament assemblies, beta-sheet nanocrystals in spider silk or tendon fascicles. These examples illustrate that the coexistence of universality and diversity – in the following referred to as the universality-diversity paradigm (UDP) – is an overarching feature in protein materials. This paradigm is a paradox: How can a structure be universal and diverse at the same time? In protein materials, the coexistence of universality and diversity is enabled by utilizing hierarchies, which serve as an additional dimension beyond the 3D or 4D physical space. This may be crucial to understand how their structure and properties are linked, and how these materials are capable of combining seemingly disparate properties such as strength and robustness. Here we illustrate how the UDP enables to unify universal building blocks and highly diversified patterns through formation of hierarchical structures that lead to multi-functional, robust yet highly adapted structures. We illustrate these concepts in an analysis of three types of intermediate filament proteins, including vimentin, lamin and keratin.
Highlights
Proteins constitute the elementary building blocks of a vast variety of biological materials such as cells, spider silk or bone, where they create multi-functional and highly robust structures, which without wasting resources - arrive at satisfactory solutions [1,2,3,4]
Even though protein materials lead to vastly complex structures such as cells, organs or organisms, an analysis of their composition reveals simple underlying mechanisms that can be classified into two major categories
These examples illustrate that the coexistence of universality and diversity is an overarching feature in protein structures
Summary
Proteins constitute the elementary building blocks of a vast variety of biological materials such as cells, spider silk or bone, where they create multi-functional and highly robust structures, which without wasting resources - arrive at satisfactory solutions [1,2,3,4]. Other features are highly specific to tissue types, such as particular filament assemblies, beta-sheet nanocrystals in spider silk or tendon fascicles 1 These examples illustrate that the coexistence of universality and diversity is an overarching feature in protein structures. We believe that this is an important concept that characterizes the structure of protein materials, in the following referred to as the universality-diversity paradigm (UDP). IFs form protein networks in the cytoskeleton of eukaryotic cell, stabilize the nuclear envelope and provide the basis for extra-cellular tissues such as hair or nails Based on this example, we show how universality and diversity are combined through hierarchical material design, leading to highly adapted, robust and multifunctional structures, governed through self-regulatory processes. We illustrate the potential impact of a better understanding of hierarchical biological protein materials in the areas of materials science, engineering and other disciplines
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