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Related Experiment Video

Updated: May 15, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Published on: September 17, 2017

Interaction signatures stabilizing the NAD(P)-binding Rossmann fold: a structure network approach.

Moitrayee Bhattacharyya1, Roopali Upadhyay, Saraswathi Vishveshwara

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

Plos One
|January 4, 2013
PubMed
Summary

Diverse protein sequences can adopt similar folds due to conserved atomic interactions. This study identifies key "spatial motifs" and "hot spots" driving the formation of the NAD(P)-binding Rossmann fold, offering a new network theory approach.

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Last Updated: May 15, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

  • Structural biology
  • Biophysics
  • Computational biology

Background:

  • Proteins with no sequence homology can adopt similar folds, challenging the direct encoding of folding pathways by amino acid sequences.
  • A limited number of protein folds are available for a vast repertoire of diverse sequences, raising questions about the factors governing fold formation.

Purpose of the Study:

  • To investigate the driving forces behind the formation of a common protein fold from diverse amino acid sequences.
  • To identify consensus structural features responsible for the adoption of the NAD(P)-binding Rossmann fold.

Main Methods:

  • Utilized network theory and graph theoretic formalism to analyze protein structures.
  • Developed a unified mathematical representation of diverse protein structures to extract topological features.
  • Applied network parameters to probe conserved atomic interactions and identify key structural elements.

Main Results:

  • Unveiled consensus structural features driving the formation of the NAD(P)-binding Rossmann fold.
  • Identified that atomic interactions at key positions are more conserved than the participating residues.
  • Proposed a
  • spatial motif
  • and
  • fold specific hot spots
  • as signature blueprints for this fold.

Conclusions:

  • The study provides a novel network-based approach to understand protein fold determination from diverse sequences.
  • The identified
  • spatial motif
  • and
  • hot spots
  • offer insights into the structural determinants of the NAD(P)-binding Rossmann fold.
  • The methodology is generalizable to other protein fold families and related problems in structural biology.