Unknown

Dataset Information

0

Small world network strategies for studying protein structures and binding.


ABSTRACT: Small world network concepts provide many new opportunities to investigate the complex three dimensional structures of protein molecules. This mini-review explores the published literature on using small-world network approaches to study protein structure, with emphasis on the different combinations of descriptors that have been tested, on studies involving ligand binding in protein-ligand complexes, and on protein-protein complexes. The benefits and success of small world network approaches, which change the focus from specific interactions to the local environment, even to non-local phenomenon, are described. The purpose is to show the different ways that small world network concepts have been used for building new computational models for studying protein structure and function, and for extending and improving existing modelling approaches.

SUBMITTER: Taylor NR 

PROVIDER: S-EPMC3962176 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

altmetric image

Publications

Small world network strategies for studying protein structures and binding.

Taylor Neil R NR  

Computational and structural biotechnology journal 20130301


Small world network concepts provide many new opportunities to investigate the complex three dimensional structures of protein molecules. This mini-review explores the published literature on using small-world network approaches to study protein structure, with emphasis on the different combinations of descriptors that have been tested, on studies involving ligand binding in protein-ligand complexes, and on protein-protein complexes. The benefits and success of small world network approaches, wh  ...[more]

Similar Datasets

| S-EPMC9974864 | biostudies-literature
| S-EPMC10609307 | biostudies-literature
| S-EPMC8542695 | biostudies-literature
| S-EPMC10216465 | biostudies-literature
| S-EPMC2816688 | biostudies-literature
| S-EPMC3536769 | biostudies-other
| S-EPMC8479126 | biostudies-literature
| S-EPMC9748015 | biostudies-literature
| S-EPMC3189935 | biostudies-literature
| S-EPMC4853440 | biostudies-literature