Protein Structure and Function: Applications of Bioinformatics Methods - John Rigden 2014

Predicting Protein Function from Surface Properties
Methods of Surface Representation

Nicholas J. Burgoyne, Richard M. Jackson

The situation where a protein's Structure is known but its function remains elusive is a common outcome of modern structural Genomics initiatives. Characterizing protein Surface Properties is just one of several approaches that can be employed to elucidate biological function. Analyzing this surface can provide valuable insights into Protein Interactions with both native biological partners and pharmacological agents. In this chapter, we introduce METABOLISM/2.html">THE CONCEPT OF the protein surface and briefly discuss widely used surface properties, as well as their application in deriving specialized metrics and Functions to evaluate protein interactions with native ligands, drugs, and other Proteins.

Before exploring what a protein's surface can reveal about its function and interactions with other molecules, it is essential to define the various representations of the surface and their significance. From the perspective of structural biology, a protein surface can be defined in several ways, each possessing distinct characteristics that dictate its Applications. The most commonly used surface representations are discussed below.



Last update: 06/08/2026

Editorial and Educational Adaptation: This material has been compiled based on the primary/original source text. The project team performed an editorial review, corrected technical inaccuracies, structured sections, and adapted the content for an educational format.

What was processed:

  • elimination of formatting defects (OCR errors, structural breaks, corrupted characters);
  • editorial organization of content;
  • standardization of terminology in accordance with academic sources;
  • verification of factual statements against the original source text.

All mentions of the author, publication year, and origin of the primary text have been preserved in accordance with the source.