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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: May 26, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Ordered and disordered proteins as nanomaterial building blocks.

Nithya Srinivasan1, Sanjay Kumar

  • 1Department of Bioengineering, University of California, Berkeley, CA, USA.

Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology
|January 11, 2012
PubMed
Summary
This summary is machine-generated.

Protein biomaterials leverage precise control over amino acid sequences and natural functions. This review explores how protein structure dictates material properties, especially in response to environmental stimuli.

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Last Updated: May 26, 2026

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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Bioinspired Materials

Background:

  • Proteins offer tunable properties for advanced biomaterials.
  • Recombinant DNA technology enables precise control over protein structure and function.
  • Nature's protein functions can be harnessed for technological applications.

Purpose of the Study:

  • To review recent advancements in protein-based biomaterials.
  • To establish structure-property relationships in protein materials.
  • To highlight the role of environmental stimuli in modulating material function.

Main Methods:

  • Review of existing literature on protein-based biomaterials.
  • Focus on elastin- and silk-like peptides with defined structures.
  • Case studies of intrinsically disordered proteins (nucleoporins, neurofilaments).

Main Results:

  • Materials derived from well-defined proteins (elastin, silk) show predictable properties.
  • Intrinsically disordered proteins offer novel material design possibilities.
  • Environmental stimuli induce conformational changes, altering material properties.

Conclusions:

  • Protein structure is a critical determinant of biomaterial properties.
  • Tunable protein sequences and environmental responsiveness enable advanced biomaterials.
  • Future research should focus on structure-function relationships and stimuli-responsive designs.