"Fuzzy Oil Drop" Model Applied to Individual Small Proteins Built of 70 Amino Acids

Overview

Journal J Mol Model

Publisher Springer

Specialty Molecular Biology

Date 2010 Jan 20

PMID 20084418

Citations 2

Authors

Katarzyna Prymula

Kinga Salapa

Irena Roterman

Affiliations

Soon will be listed here.

Abstract

The proteins composed of short polypeptides (about 70 amino acid residues) representing the following functional groups (according to PDB notation): growth hormones, serine protease inhibitors, antifreeze proteins, chaperones and proteins of unknown function, were selected for structural and functional analysis. Classification based on the distribution of hydrophobicity in terms of deficiency/excess as the measure of structural and functional specificity is presented. The experimentally observed distribution of hydrophobicity in the protein body is compared to the idealized one expressed by a three-dimensional Gauss function. The differences between these two distributions reveal the specificity of structural/functional characteristics of the protein. The residues of hydrophobicity deficiency versus the idealized distribution are assumed to indicate cavities with the potential to bind ligands, while the residues of hydrophobicity excess are interpreted as potentially participating in protein-protein complexation. The distribution of hydrophobicity irregularity seems to be specific for particular structures and functions of proteins. A comparative analysis of such profiles is carried out to identify the potential biological activity of proteins of unknown function.

Citing Articles

Fuzzy oil drop model to interpret the structure of antifreeze proteins and their mutants.

Banach M, Prymula K, Jurkowski W, Konieczny L, Roterman I J Mol Model. 2011; 18(1):229-37.

PMID: 21523554 PMC: 3249532. DOI: 10.1007/s00894-011-1033-4.

Searching in microbial genomes for encoded small proteins.

Boekhorst J, Wilson G, Siezen R Microb Biotechnol. 2011; 4(3):308-13.

PMID: 21518296 PMC: 3818988. DOI: 10.1111/j.1751-7915.2011.00261.x.

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