Functional and structural characterization of a protein based on analysis of its hydrogen bonding network by hydrogen bonding plot

Arch Biochem Biophys. 2007 May 15;461(2):225-34. doi: 10.1016/j.abb.2007.02.020. Epub 2007 Mar 12.

Abstract

Knowledge of the relationship between protein's structure and its dynamic behavior is essential for understanding protein function. In this study, the description of a protein three-dimensional structure as a network of hydrogen bonding interactions (HB plot) is introduced as a tool for exploring protein structure and function. HB plot offers a simple way of analyzing protein secondary and tertiary structure. Moreover, hydrogen bonds stabilizing secondary structural elements and those formed between distant amino residues--defined as tertiary hydrogen bonds--can be easily distinguished in HB plot, thus, amino acid residues involved in stabilizing protein structure and function can be easily identified. By analyzing the network of tertiary interactions the possible spread of information within a protein can be investigated as well. The alteration in tertiary hydrogen bonding network during conformational transitions were investigated through case studies; and showed the applicability of HB plot in exploring mechanistic details in proteins.

Publication types

  • Comparative Study

MeSH terms

  • Algorithms
  • Animals
  • Aryl Hydrocarbon Hydroxylases / analysis
  • Aryl Hydrocarbon Hydroxylases / chemistry*
  • Aryl Hydrocarbon Hydroxylases / physiology*
  • Cytochrome P450 Family 2
  • Hydrogen Bonding
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rabbits
  • Structure-Activity Relationship

Substances

  • Aryl Hydrocarbon Hydroxylases
  • Cytochrome P450 Family 2
  • cytochrome P-450 CYP2B4 (rabbit)