Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach

R Brahma, H Raghuraman - Emerging topics in life sciences, 2021 - portlandpress.com
Protein hydration dynamics plays an important role in many physiological processes since
protein fluctuations, slow solvation, and the dynamics of hydrating water are all intrinsically …

The red edge excitation shift phenomenon can be used to unmask protein structural ensembles: implications for NEMO–ubiquitin interactions

DAM Catici, HE Amos, Y Yang… - The FEBS …, 2016 - Wiley Online Library
To understand complex molecular interactions, it is necessary to account for molecular
flexibility and the available equilibrium of conformational states. Only a small number of …

Multiple functions of spectrin: convergent effects

D Bose, A Chakrabarti - The Journal of membrane biology, 2020 - Springer
Spectrin is a multifunctional, multi-domain protein most well known in the membrane
skeleton of mature human erythrocytes. Here we review the literature on the crosstalk of the …

Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift

MJ Knight, RE Woolley, A Kwok, S Parsons… - Biochemical …, 2020 - portlandpress.com
Among the major challenges in the development of biopharmaceuticals are structural
heterogeneity and aggregation. The development of a successful therapeutic monoclonal …

Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition

AK Warrender, J Pan, C Pudney… - Journal of the …, 2023 - royalsocietypublishing.org
Red edge excitation shift (REES) spectroscopy relies on the unique emission profiles of
fluorophore–solvent interactions to profile protein molecular dynamics. Recently, we …

Effect of pH on stability, conformation, and chaperone activity of erythroid & non-erythroid spectrin

D Bose, M Patra, A Chakrabarti - … et Biophysica Acta (BBA)-Proteins and …, 2017 - Elsevier
Spectrin, a major component of the eukaryotic membrane skeleton, has been shown to have
chaperone like activity. Here we investigate the pH induced changes in the structure and …

Structural Flexibility of Proteins Dramatically Alters Membrane Stability─ A Novel Aspect of Lipid–Protein Interaction

RP Giri, MK Mukhopadhyay, MK Sanyal… - The Journal of …, 2022 - ACS Publications
Protein isoforms are structural variants with changes in the overall flexibility predominantly at
the tertiary level. For membrane associated proteins, such structural flexibility or rigidity …

Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils

B Pastrello, GC dos Santos, LC da Silva-Filho… - Dyes and …, 2020 - Elsevier
A novel aminoquinoline derivative (AQ) was synthesized and applied as a solvatochromic
fluorescent probe to study proteins and their alterations. AQ is not fluorescent in aqueous …

Constrained dynamics of the sole tryptophan in the third intracellular loop of the serotonin1A receptor

S Pal, R Aute, P Sarkar, S Bose, MV Deshmukh… - Biophysical …, 2018 - Elsevier
G protein-coupled receptors (GPCRs) are major signaling proteins in eukaryotic cells and
are important drug targets. In spite of their role in GPCR function, the extramembranous …

Comparative analysis of tryptophan dynamics in spectrin and its constituent domains: Insights from fluorescence

S Pal, D Bose, A Chakrabarti… - The Journal of Physical …, 2021 - ACS Publications
Spectrin is a cytoskeletal protein ubiquitous in metazoan cells that acts as a liaison between
the plasma membrane and the cellular interior and imparts mechanical stability to the …