Báo cáo khoa học: Short hydrogen bonds in proteins Sathyapriya Rajagopal and Saraswathi Vishveshwara

Short Hydrogen Bonds in Proteins

Authors: Sathyapriya Rajagopal and Saraswathi Vishveshwara

Field: Molecular Biophysics

Document Content:
This study systematically characterizes short hydrogen bonds (SHBs) in a nonredundant dataset of protein structures. It reveals that SHBs are prevalent across various regions of protein chains, including backbones, side chains, and different secondary structural elements like helices, strands, and turns. The research highlights that both charged and neutral atoms contribute significantly to SHBs, suggesting their formation is driven by enhanced strength or geometrical constraints. The work also investigates the role of SHBs in protein structure stabilization and function, including their presence in enzyme active sites and their contribution to tertiary structure integrity. The paper details the classification, statistics, and environmental preferences of SHBs, as well as their involvement in multiple hydrogen bond formations and specific interactions like sulfur-containing SHBs.

Detailed Table of Contents:

• Keywords
• Correspondence
• Abstract
• Introduction
• Results and Discussion
  • Dataset validation
  • Classification and statistics of SHBs in proteins
  • Amino acid preferences
  • Environment of the backbone donors and acceptors
  • Multiple hydrogen bonds
  • Sulfur-containing SHBs
  • SHBs mediating structural constraints in protein structures
• Conclusions
• Experimental procedures
• Acknowledgements
• References
• Supplementary Material