Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

By directly probing the photolyzed NO from MbNO at physiological conditions, the rebinding trajectories of the photoproduct were obtained, from which we found that a time-dependent barrier arising from protein relaxation on the same time scale as that of the rebinding process is responsible for the NO nonexponential rebinding.

Download full-text PDF

Source
http://dx.doi.org/10.1021/ja0502270DOI Listing

Publication Analysis

Top Keywords

protein conformation-induced
4
conformation-induced modulation
4
modulation ligand
4
ligand binding
4
binding kinetics
4
kinetics femtosecond
4
femtosecond mid-ir
4
mid-ir study
4
study nitric
4
nitric oxide
4

Similar Publications

Fluorogen-Activating Human Serum Albumin for Mitochondrial Nanoscale Imaging.

Adv Mater

September 2025

State Key Laboratory of Flexible Electronics (LoFE) & Institute of Flexible Electronics (IFE), Xiamen University, Xiamen, 361102, China.

Fluorescence nanoscopy of living cells employs contrast agents to reveal intrinsic correlations between mitochondrial dynamics and functions at the molecular level. However, regular mitochondrial fluorophores usually present poor photostability, low brightness, non-specific inhibitory effects, high phototoxicity, and rapid photobleaching, which have hindered the use of these tools to capture the intricate dynamic features of mitochondria. Herein, we engineered a fluorogen-activating protein (FAP), AmpHecy@HSA, a non-covalent self-assembly of HSA and amphiphilic hemicyanine (AmpHecy) fluorophore, with exceptional cell permeability, long-lasting photostability, high brightness/fluorogenicity, and minimal phototoxicity.

View Article and Find Full Text PDF

Distinct oligomeric assemblies of STING induced by non-nucleotide agonists.

Nat Commun

April 2025

Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, USA.

STING plays essential roles coordinating innate immune responses to processes that range from pathogenic infection to genomic instability. Its adaptor function is activated by cyclic dinucleotide (CDN) secondary messengers originating from self (2'3'-cGAMP) or bacterial sources (3'3'-CDNs). Different classes of CDNs possess distinct binding modes, stabilizing STING's ligand-binding domain (LBD) in either a closed or open conformation.

View Article and Find Full Text PDF

Discovery of non-electrophilic TRPA1 channel agonists with anti-nociceptive effects via rapid current desensitization.

Eur J Med Chem

July 2025

Departments of Pharmacology and Pharmaceutical Analysis, School of Pharmacy, Qingdao University Medical College, Qingdao, 266073, China; Institute of Innovative Drug Discovery, Qingdao University Medical College, 38 Dengzhou Road, Qingdao, 266021, China.

Desensitizing transient receptor potential ankyrin 1 (TRPA1) cation channel through agonists emerges as an effective strategy for developing analgesics. Many TRPA1 agonists are electrophilic irritants, including BITC and iodoacetamide (IA), which covalently bind to cysteine residues in the cytoplasmic region of the channel. The electrophile JT010 is also recognized as a potent TRPA1 agonist via covalent modification of Cys621, whose irritant effects have been confirmed in humans, highlighting a commonly undesirable property of these electrophilic agonists.

View Article and Find Full Text PDF

Ponceau 4R induces aggregation in human serum albumin and morin acts as an anti-aggregating agent against dye induced aggregates.

Spectrochim Acta A Mol Biomol Spectrosc

July 2025

Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, U.P., India. Electronic address:

Aggregation of proteins occurs because of improper protein folding and is responsible for the development of multiple severe maladies such as Type II diabetes mellitus, Parkison's, Huntington's, and spongiform encephalopathy. In the current work, the interaction and aggregation of human serum albumin (HSA) in the presence of the food colorant Ponceau 4R at pH 2.0 was evaluated using multiple in-silico and multi-spectroscopic approaches.

View Article and Find Full Text PDF

In this study, the role of phosphorylation in the liquid-liquid phase separation (LLPS) of tau, the underlying driving forces, and the potential implications of this separation on protein conformation and subsequent protein aggregation were investigated. We compared in vivo-produced phosphorylated tau (p-tau) and nonphosphorylated tau under different coacervation conditions without adding crowding agents. Our findings revealed that spontaneous phase separation occurs exclusively in p-tau, triggered by a temperature shift from 4 °C to room temperature, and is driven by electrostatic and hydrophobic interactions.

View Article and Find Full Text PDF