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Construction and Characterization of a Novel Vocal Fold Bioreactor

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55 Years of the Rossmann Fold

Woong-Hee Shin¹, Daisuke Kihara^2,3

¹Department of Biological Science, Purdue University, West Lafayette, IN, USA.

Methods in Molecular Biology (Clifton, N.J.)

|April 5, 2019

Summary

The Rossmann fold, a common protein structure, is explored 55 years after its discovery. Its prevalence in databases and genomes, and potential for protein engineering, are discussed.

Area of Science:

Structural Biology
Protein Science
Bioinformatics

Background:

The Rossmann fold is a prevalent protein structural motif.
It consists of alternating beta-strands and alpha-helices forming a layered structure.

Purpose of the Study:

To provide a comprehensive overview of the Rossmann fold.
To examine its occurrence in major protein databases and genomes.
To discuss its significance in protein engineering.

Main Methods:

Literature review and database analysis (SCOP, CATH).
Bioinformatic analysis of genomic occurrences.
Discussion of protein engineering implications.

Main Results:

The Rossmann fold has been recognized for 55 years.
It is widely represented in protein classification databases and across various genomes.
Site-directed mutagenesis can modify its ligand-binding properties.

Conclusions:

The Rossmann fold remains a fundamental and extensively studied protein domain.
Its widespread distribution highlights its evolutionary importance.
The fold is a promising target for protein engineering applications.

Keywords:

CATH Nucleotide-binding fold Protein engineering Protein fold Protein structure classification Rossmann fold SCOP

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