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Rajitha Rajeshwar T

Explore the profile of Rajitha Rajeshwar T including associated specialties, affiliations and a list of published articles. Areas
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Articles 9
Citations 25
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Recent Articles
1.
Conthagamage U, Rajeshwar T R, van der Ham S, Akhtar N, Davis M, Jayawardana S, et al.
Commun Chem . 2024 Nov; 7(1):255. PMID: 39516242
Rotaxanes equipped with actuators hold great potential for developing highly functional molecular machines. Such systems could significantly enhance our ability to study and manipulate biological and artificial membranes. Here, we...
2.
Rajeshwar T R, Demerdash O, Smith J
Front Immunol . 2024 Sep; 15:1426173. PMID: 39221256
Artificial-intelligence and machine-learning (AI/ML) approaches to predicting T-cell receptor (TCR)-epitope specificity achieve high performance metrics on test datasets which include sequences that are also part of the training set but...
3.
Agarwal R, Rajeshwar T R, Smith J
J Chem Inf Model . 2023 Nov; 63(23):7444-7452. PMID: 37972310
Structure-based virtual high-throughput screening is used in early-stage drug discovery. Over the years, docking protocols and scoring functions for protein-ligand complexes have evolved to improve the accuracy in the computation...
4.
Poudel B, Rajeshwar T R, Vanegas J
Nat Commun . 2023 Aug; 14(1):4690. PMID: 37542033
The Angiotensin II Type 1 (AT1) receptor is one of the most widely studied GPCRs within the context of biased signaling. While the AT1 receptor is activated by agonists such...
5.
Rajeshwar T R, Smith J
Proteins . 2022 Apr; 90(9):1645-1654. PMID: 35403257
The startling diversity in αβ T-cell receptor (TCR) sequences and structures complicates molecular-level analyses of the specificity and sensitivity determining T-cell immunogenicity. A number of three-dimensional (3D) structures are now...
6.
Rajeshwar T R, Saharay M, Smith J, Krishnan M
J Phys Chem B . 2021 Aug; 125(34):9641-9651. PMID: 34423989
The heterogeneous fast side-chain dynamics of proteins plays crucial roles in molecular recognition and binding. Site-specific NMR experiments quantify these motions by measuring the model-free order parameter () on a...
7.
Rajeshwar T R, Anishkin A, Sukharev S, Vanegas J
Biophys J . 2020 Dec; 120(2):232-242. PMID: 33333032
Membrane tension perceived by mechanosensitive (MS) proteins mediates cellular responses to mechanical stimuli and osmotic stresses, and it also guides multiple biological functions including cardiovascular control and development. In bacteria,...
8.
Rajeshwar T R, Krishnan M
J Phys Chem B . 2017 Apr; 121(20):5174-5186. PMID: 28452484
A novel approach to accurately determine residue-specific noncovalent interaction strengths (ξ) of proteins from NMR-measured fast side chain motional parameters (O) is presented. By probing the environmental sensitivity of side...
9.
Rajeshwar T R, Smith J, Krishnan M
J Am Chem Soc . 2014 May; 136(24):8590-605. PMID: 24844417
Proteins display characteristic dynamical signatures that appear to be universal across all proteins regardless of topology and size. Here, we systematically characterize the universal features of fast side chain motions...