Ganesan P

VIT Business School

Vellore Campus

Ramalingam R.

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Journal of Cellular Biochemistry

Pathological role of a point mutation (T315I) in BCR-ABL1 protein-A computational insight

Tumor Biology

Impact of point mutation P29S in RAC1 on tumorigenesis

Cell Biochemistry and Biophysics

Biophysical Aspect of Huntingtin Protein During polyQ: An In Silico Insight

Arginine to histidine mutation at position 132 (R132H) in isocitrate dehydrogenase 1 (IDH1) led to reduced affinity of the respective enzymes for isocitrate and increased affinity for α-ketoglutarate (AKG) and NADPH.

Molecular BioSystems

Structural analysis of oncogenic mutation of isocitrate dehydrogenase 1

Candida antarcticalipase B (CALB) is a known stable and highly active enzyme used widely in biodiesel synthesis. In this work, the stability of native (4K6G) and mutant (4K5Q) CALB was studied through various structural parameters using conformational sampling approach. The contours of polar surface area and surface area of mutant CALB were 11357.67 Å2and 30007.4 Å2, respectively, showing an enhanced stability compared to native CALB with a statistically significantPvalue of < 0.0001. Moreover, simulated thermal denaturation of CALB, a process involving dilution of hydrogen bond, significantly shielded against different intervals of energy application in mutant CALB revealing its augmentation of structural rigidity against native CALB. Finally, computational docking analysis showed an increase in the binding affinity of CALB and its substrate (triglyceride) in mutant CALB with Atomic Contact Energy (ACE) of −91.23 kcal/mol compared to native CALB (ACE of −70.3 kcal/mol). The computational observations proposed that the use of mutant CALB (4K5Q) could serve as a best template for production of biodiesel in the future. Additionally, it can also be used as a template to identify efficient thermostable lipases through further mutations.

Fulltext

Biochemistry Research International

Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs

Investigation of structural stability and functionality of homodimeric gramicidin towards peptide‐based drug: a molecular simulation approach

Journal	Data powered by TypesetJournal of Cellular Biochemistry
Publisher	Data powered by TypesetWiley
ISSN	0730-2312
Open Access	0