Small protein–protein interfaces rich in electrostatic are often linked to regulatory function-Reference-Cited by-同舟云学术

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Small protein–protein interfaces rich in electrostatic are often linked to regulatory function

Published:2019-09-09 Issue:11 Volume:38 Page:3260-3279
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Nilofer Christina¹²,Sukhwal Anshul³,Mohanapriya Arumugam²,Sakharkar Meena Kishore⁴,Kangueane Pandjassarame¹

Affiliation:

1. Biomedical Informatics (P) Ltd., Pondicherry, India;

2. School of Biosciences & Technology, VIT University, Vellore, Tamil Nadu, India;

3. National Centre for Biological Sciences (NCBS), Bangalore, India;

4. College of Pharmacy and Nutrition, Saskatchewan University, Saskatchewan, Canada

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1657040

Reference57 articles.

1. A Dissection of Specific and Non-specific Protein–Protein Interfaces

2. Transient protein-protein interface prediction: datasets, features, algorithms, and the RAD-T predictor

3. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?

4. Dissecting protein-protein recognition sites

5. Principles of protein–protein recognition

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2. Computed Protein–Protein Enthalpy Signatures as a Tool for Identifying Conformation Sampling Problems;Journal of Chemical Information and Modeling;2023-09-28

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4. An exhaustive review of computational prediction techniques for PPI sites, protein locations, and protein functions;Network Modeling Analysis in Health Informatics and Bioinformatics;2023-08-31

5. Electrostatic Interactions Contribute to the Overall Structural Stability in Small Interfaces of Corona Viral Spike Glycoproteins;Biomedical and Pharmacology Journal;2022-03-31

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