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Protein Folding

Protein Folding

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

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...

Protein Organization

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....

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Related Experiment Video

Updated: Jul 29, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Towards sequence-based principles for protein phase separation predictions.

Michele Vendruscolo¹, Monika Fuxreiter²

¹Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

Current Opinion in Chemical Biology

|May 19, 2023

Summary

This summary is machine-generated.

Protein sequences can predict phase separation into liquid or solid states. Understanding entropic contributions is key to advancing these predictive methods for biomolecular condensates.

Keywords:

Protein aggregation Protein interactions Protein phase separation Sequence-based predictions

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Last Updated: Jul 29, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

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Published on: June 19, 2012

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Protein phase separation drives the formation of essential biomolecular condensates.
Amino acid sequences dictate not only protein folding but also phase separation into liquid-like (droplet) and solid-like (amyloid) states.

Purpose of the Study:

To review sequence-based methods for predicting protein phase separation propensity.
To highlight the importance of entropic contributions in stabilizing the droplet state.

Main Methods:

Review of current sequence-based prediction principles.
Discussion of progress in estimating entropic contributions.

Main Results:

Entropic contributions are crucial for stabilizing the liquid-like droplet state compared to native and amyloid states.
Recent advancements have been made in quantifying these entropic contributions.

Conclusions:

Sequence-based prediction of protein phase separation is advancing.
Future work should integrate quantitative in vivo characterizations with predictive models.