Identification of potential mutational hotspots in serratiopeptidase to address its poor pH tolerance issue-Reference-Cited by-同舟云学术

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Identification of potential mutational hotspots in serratiopeptidase to address its poor pH tolerance issue

Published:2022-10-28 Issue: Volume: Page:1-13
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Dhiman Ankita¹²³,Purohit Rituraj¹²³

Affiliation:

1. Structural Bioinformatics Lab, CSIR-Institute of Himalayan Bioresource Technology (CSIR-IHBT), Palampur, Himachal Pradesh, India

2. Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology (CSIR-IHBT), Palampur, Himachal Pradesh, India

3. Academy of Scientific & Innovative Research (AcSIR), Ghaziabad, India

Funder

CSIR-National Botanical Research Institute

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2022.2137699

Reference60 articles.

1. Electrostatics of nanosystems: Application to microtubules and the ribosome

2. Normal Mode Analysis as a Routine Part of a Structural Investigation

3. Crystal Structure of the 50 Kda Metallo Protease from Serratia marcescens

4. Crystal Structure of a Complex BetweenSerratia marcescensMetallo-protease and an Inhibitor fromErwinia chrysanthemi

5. Molecular dynamics with coupling to an external bath

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3. Targeting tachykinin peptides involved in viral infections through in silico approach: Screening the unforeseen potency of serratiopeptidase;Journal of Molecular Liquids;2023-12

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