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Updated: Jul 11, 2026

Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins

Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins

Published on: June 11, 2015

Fold predictions for bacterial genomes.

K Pawlowski¹, L Rychlewski, B Zhang

¹AstraZeneca R&D Lund, Lund, S-221 87, Sweden.

Journal of Structural Biology

|September 12, 2001

Summary

This summary is machine-generated.

Protein structure prediction aids in assigning protein folds for new genomes. This review explores advancements and future directions for understanding protein functions in newly sequenced genomes.

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Area of Science:

Structural bioinformatics
Genomics
Computational biology

Background:

Protein structure prediction is crucial for understanding protein function.
Newly sequenced genomes present opportunities for large-scale fold assignment.
Existing methods require enhancement for deeper functional insights.

Purpose of the Study:

To survey current fold assignment projects for newly sequenced genomes.
To discuss the development of tools for functional understanding beyond simple assignments.
To address challenges and future perspectives in protein structure prediction.

Main Methods:

Review of fold assignment projects for Escherichia coli proteins.
Discussion of domain prediction, transmembrane regions, and flexible region predictions.
Analysis of cross-correlation between different prediction servers.

Main Results:

Fold assignment is a key application in protein structure prediction.
Advancements are needed to move beyond basic assignments to functional understanding.
Database growth significantly influences prediction success.

Conclusions:

Developing advanced tools is essential for functional genomics.
Addressing domain and complementary predictions is critical.
Future research should focus on novel methods and massive data projects.