Over the past years, native mass spectrometry and ion mobility have grown into techniques that are widely applicable to the study of aspects of protein structure. More recently, it has become apparent that this approach provides a very promising avenue for the investigation of integral membrane proteins in lipid or detergent environments.In this chapter, we discuss applications of native mass spectrometry and ion mobility in membrane protein research-what is important to take into consideration when working with membrane proteins, and what the requirements are for sample preparation for native mass spectrometry. Furthermore, we will discuss the types of information provided by the measurements, including the oligomeric state, subunit composition and stoichiometry, interactions with detergents or lipids, conformational transitions, and the binding and structural effect of ligands and drugs.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/978-1-4939-7151-0_11 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Optimizing In Vitro Propagation of Schönland Using Leaf, Root, and Inflorescence.
Plants (Basel)
January 2025
Instituto de Bioingeniería, Universidad Miguel Hernández, 03202 Elche, Spain.
, a species native to South Africa, is characterized by its limited growth and scarcity, contributing to high production costs. Countries like China and Turkey are known for exporting globally. Tissue culture offers an efficient method for mass-producing unique and beautiful species such as This study tested Murashige and Skoog (MS) basal media supplemented with various concentrations of IBA (0.
View Article and Find Full Text PDFMultivariate Statistical Analyses of the Temporal Variation in the Chemical Composition of the Essential Oil of in Cyprus.
Molecules
January 2025
Department of Pharmaceutical Botany, Faculty of Pharmacy, Near East University, 99010 Nicosia, Cyprus.
The genus L'Hér., is native to Australia with 61 introduced taxa in Cyprus, including Luehm., which has a wide distribution on the island.
View Article and Find Full Text PDFThe Use of Dansyl Chloride to Probe Protein Structure and Dynamics.
Int J Mol Sci
January 2025
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Dansyl labeling is a widely used approach for enhancing the detection of small molecules by UV spectroscopy and mass spectrometry. It has been successfully applied to identify and quantify a variety of biological and environmental specimens. Despite clear advantages, the dansylation reaction has found very few applications in the study of proteins.
View Article and Find Full Text PDFImpact of Ultrasonic-Assisted Preparation of Water Caltrop Starch-Lipid Complex: Structural and Physicochemical Properties.
Foods
January 2025
Department of Food Science and Biotechnology, National Chung Hsing University, 145 Xingda Road, Taichung 40227, Taiwan.
This study investigates the effect of ultrasonic-assisted preparation on the structural and physicochemical properties of water caltrop starch-palmitic acid complexes as a function of ultrasound intensity and treatment time. All samples exhibited the characteristic birefringence of starch-lipid complexes under the polarized microscope, and flake-like and irregular structure under scanning electron microscope (SEM), indicating the formation of complexes through ultrasonic-assisted preparation. X-ray diffraction pattern further confirmed the transition from the original A-type structure for native starch to V-type structure for starch-lipid complexes, and the relative crystallinity of starch-lipid complexes increased as the ultrasound intensity and treatment time increased.
View Article and Find Full Text PDFEnergy Resolved Mass Spectrometry Data from Surfaced Induced Dissociation Improves Prediction of Protein Complex Structure.
Anal Chem
January 2025
Department of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio 43210, United States.
Native Mass Spectrometry (nMS) is a versatile technique for elucidating protein structure. Surface-Induced Dissociation (SID) is an activation method in tandem MS predominantly employed for determining protein complex stoichiometry alongside information about interface strengths. SID-nMS data can be collected over a range of acceleration energies, yielding Energy Resolved Mass Spectrometry (ERMS) data.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!