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Intrinsically Disordered Proteins

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...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

Signal Sequences and Sorting Receptors

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Related Experiment Video

Updated: Apr 3, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers.

Felipe García Quiroz¹, Ashutosh Chilkoti¹

¹Department of Biomedical Engineering, Duke University, Durham, North Carolina 27708, USA.

Nature Materials

|September 22, 2015

Summary

This summary is machine-generated.

Scientists designed proteins with tunable phase transitions, controlling self-assembly. This work provides methods to predict and engineer protein phase behavior based on amino acid sequences.

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Area of Science:

Biochemistry
Materials Science
Protein Engineering

Background:

Aqueous phase transitions in proteins and synthetic polymers drive self-assembly in biological and artificial systems.
Understanding how amino acid sequences dictate protein phase behavior is crucial but largely unknown.

Purpose of the Study:

To investigate the encoding of phase behavior within protein amino acid sequences.
To design proteins exhibiting tunable lower critical solution temperature (LCST) and upper critical solution temperature (UCST) transitions.

Main Methods:

Synthesis of intrinsically disordered, repeat proteins to test hypothesized phase-encoding motifs.
Mutation analysis at the repeat level to assess impact on phase behavior.
Development of heuristics for proteome-level identification and design of phase-behaving proteins.

Main Results:

Designed proteins demonstrated tunable LCST and UCST phase transitions in physiological solutions.
Key residue mutations abolished or altered protein phase behavior, indicating sequence-level control.
Heuristics were established for identifying and designing novel protein polymers with specific phase transition properties.

Conclusions:

Protein phase behavior can be predicted and encoded at the amino acid sequence level.
This research lays the groundwork for designing novel protein-based materials with controlled self-assembly properties.