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Measuring the Equilibrium Spreading Pressure-A Tale of Three Amphiphiles.
Molecules
August 2024
School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London E1 4NS, UK.
A surfactant's equilibrium spreading pressure (ESP) is the maximum decrease in surface tension achievable at equilibrium below the Krafft point. Difficulties in measuring the ESP have been noted previously but no well-established experimental protocols to overcome them exist. We present a case study of three solid amphiphiles with different propensities to spread on the air-water interface.
View Article and Find Full Text PDFA finely balanced order-disorder equilibrium sculpts the folding-binding landscape of an antibiotic sequestering protein.
Proc Natl Acad Sci U S A
May 2024
Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India.
TipA, a MerR family transcription factor from , promotes antibiotic resistance by sequestering broad-spectrum thiopeptide-based antibiotics, thus counteracting their inhibitory effect on ribosomes. TipAS, a minimal binding motif which is expressed as an isoform of TipA, harbors a partially disordered N-terminal subdomain that folds upon binding multiple antibiotics. The extent and nature of the underlying molecular heterogeneity in TipAS that shapes its promiscuous folding-function landscape is an open question and is critical for understanding antibiotic-sequestration mechanisms.
View Article and Find Full Text PDF[Comparison of two capillary electrophoresis methods for aptamer-protein affinity characterization].
Se Pu
September 2020
State Key Laboratory of Toxicology and Medical Countermeasures, and Institute of Toxicology and Pharmacology, Academy of Military Medical Sciences, Beijing 100850, China.
Affinity interaction characterization is a prerequisite for understanding the specific binding of nucleic acid aptamers to their target molecules and consequently their appropriate applications. The CE technique provides a simple and multi-mode approach to such a characterization, but different results obtained from multiple modes and systems lead to limited reliability and further applications. Thus, there is an urgent need to develop systematic comparison approaches of multi-mode applications in CE, which would allow a better investigation of the affinity between aptamers and target molecules.
View Article and Find Full Text PDFMolecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.
ACS Chem Biol
July 2021
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, SE-75123 Uppsala, Sweden.
Intrinsically disordered regions in proteins often function as binding motifs in protein-protein interactions. The mechanistic aspects and molecular details of such coupled binding and folding reactions, which involve formation of multiple noncovalent bonds, have been broadly studied theoretically, but experimental data are scarce. Here, using a combination of protein semisynthesis to incorporate phosphorylated amino acids, backbone amide-to-ester modifications, side chain substitutions, and binding kinetics, we examined the interaction between the intrinsically disordered motif of amyloid precursor protein (APP) and the phosphotyrosine binding (PTB) domain of Mint2.
View Article and Find Full Text PDFUnderstanding the Thermal Denaturation of Myoglobin with IMS-MS: Evidence for Multiple Stable Structures and Trapped Pre-equilibrium States.
J Am Soc Mass Spectrom
January 2021
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Thermal denaturation of holomyoglobin (hMb) in solution (10 mM ammonium acetate at pH = 4.5, 6.8, and 9.
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