Skip NavigationSkip to Content
Return Return to Search Results

Structural complexity and population analysis of hydrogen-bonded networks in proteins

  1. Author:
    Arteca, G. A.
    Luo, X.

  2. Author Address

    Arteca GA Laurentian Univ, Dept Chim & Biochim Ramsey Lake Rd Sudbury ON P3E 2C6 Canada Laurentian Univ, Dept Chim & Biochim Sudbury ON P3E 2C6 Canada NCI, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Theochem-Journal of Molecular Structure
    1. 501
    2. Pages: 479-493
  4. Type of Article: Article
  1. Abstract:

    We discuss an approach to characterize the structural organization of hydrogen-bonded networks formed by proteins. Emphasis is made on global descriptors, deriving inspiration from percolation theory, which convey size and connectivity. Our goal is to test whether there is a pattern of network features shared by hydrated proteins. To this end, we have compared a number of experimental structures where detailed information on hydrogen bond geometry is available. For the selected proteins, we have studied the following population properties associated with network topology: (a) the number of hydrogen atoms embedded in water-only, protein-only, and water-protein networks; (b) the total number and size distribution of the maximum-connected components of these networks. Using these properties, we compute two order parameters of network complexity. These parameters allow one to compare the hydrogen-bonding patterns in hydrated (or dry) proteins with those of bulk water. Our results suggest a general relation between these order parameters in proteins, as well as "avoided" regions with molecular shape features that may not be reachable in actual hydration-shell networks. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 60]

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel