Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Categorization of hotspots into three types - weak, moderate and strong to distinguish protein-protein versus protein-peptide interactions.

Journal of biomolecular structure & dynamics - 1 Nov 2024

Kumar A Kiran, Rathore R S

Abstract excerpt

Protein-protein and protein-peptide interactions (PPI and PPepI) belong to a similar category of interactions, yet seemingly subtle differences exist among them. To characterize differences between protein-protein (PP) and protein-peptide (PPep) interactions, we have focussed on two important classes of residues-hotspot and anchor residues. Using implicit solvation-based free energy calculations, a very...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Peptides

Share to Protein Binding

Share to Proteins

Share to Thermodynamics

Source

Identifiers

PMID: 37649387
DOI: 10.1080/07391102.2023.2252077

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Categorization of hotspots into three types - weak, moderate and strong to distinguish protein-protein versus protein-peptide interactions.PMID 37649387Read ↗

PIIMS Server: A Web Server for Mutation Hotspot Scanning at the Protein-Protein Interface.Semantic proximity Read ↗

Characterizing changes in the rate of protein-protein dissociation upon interface mutation using hotspot energy and organization.Semantic proximity Read ↗

Protein-protein interactions; coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking.Semantic proximity Read ↗

DrugScorePPI webserver: fast and accurate in silico alanine scanning for scoring protein-protein interactions.Semantic proximity Read ↗

Hot spots in protein-protein interfaces: towards drug discovery.Semantic proximity Read ↗

Context-based identification of protein-protein interfaces and "hot-spot" residues.Semantic proximity Read ↗

Computational alanine scanning of protein-protein interfaces.Semantic proximity Read ↗

Structure-based method for analyzing protein-protein interfaces.Semantic proximity Read ↗

Co-Occurring Atomic Contacts for the Characterization of Protein Binding Hot Spots.Semantic proximity Read ↗

Techniques for Developing Reliable Machine Learning Classifiers Applied to Understanding and Predicting Protein:Protein Interaction Hot SpotsSemantic proximity Read ↗

Integrating water exclusion theory into β contacts to predict binding free energy changes and binding hot spots.Semantic proximity Read ↗

Rosetta custom score functions accurately predict ΔΔG of mutations at protein-protein interfaces using machine learning.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.