Read Books Online and Download eBooks, EPub, PDF, Mobi, Kindle, Text Full Free.
Investigating Native State Protein Dynamics Through Simulations Of Hydrogen Exchange Mass Spectrometry And Bayesian Analysis Of Experimental Data
Download Investigating Native State Protein Dynamics Through Simulations Of Hydrogen Exchange Mass Spectrometry And Bayesian Analysis Of Experimental Data full books in PDF, epub, and Kindle. Read online Investigating Native State Protein Dynamics Through Simulations Of Hydrogen Exchange Mass Spectrometry And Bayesian Analysis Of Experimental Data ebook anywhere anytime directly on your device. Fast Download speed and no annoying ads. We cannot guarantee that every ebooks is available!
Book Synopsis Investigating Native-state Protein Dynamics Through Simulations of Hydrogen Exchange Mass Spectrometry and Bayesian Analysis of Experimental Data by : John C. Strahan
Download or read book Investigating Native-state Protein Dynamics Through Simulations of Hydrogen Exchange Mass Spectrometry and Bayesian Analysis of Experimental Data written by John C. Strahan and published by . This book was released on 2018 with total page 106 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Investigating Native-state Protein Dynamics Through Simulations of Hydrogen Exchange Mass Spectrometry by : Nevon Song
Download or read book Investigating Native-state Protein Dynamics Through Simulations of Hydrogen Exchange Mass Spectrometry written by Nevon Song and published by . This book was released on 2016 with total page 212 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Hydrogen Exchange Mass Spectrometry of Proteins by : David D. Weis
Download or read book Hydrogen Exchange Mass Spectrometry of Proteins written by David D. Weis and published by John Wiley & Sons. This book was released on 2016-03-21 with total page 422 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.
Book Synopsis Hydrogen/deuterium Exchange Mass Spectrometry as a Technology Platform for Studying Conformational Dynamics in Large Protein Complexes by : Sasidhar N. Nirudodhi
Download or read book Hydrogen/deuterium Exchange Mass Spectrometry as a Technology Platform for Studying Conformational Dynamics in Large Protein Complexes written by Sasidhar N. Nirudodhi and published by . This book was released on 2013 with total page 199 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteins are essential to all biological systems. Proteins participate in numerous cellular processes by interacting with other proteins, other metabolites and membranes in a dynamic environment. Studying the structural and conformational properties of proteins in the solution phase is necessary to understand their protein folding and interaction dynamics. This research project focused on the development and application of hydrogen deuterium exchange mass spectrometry (HDX-MS) technology for studying the conformational dynamics of large multi-subunit protein systems. HDX-MS studies were conducted on representative proteins of two much researched protein families, namely Peroxiredoxins (Prxs) and Cullin Ring Ligases (CRLs). As part of this research we implemented tandem mass spectrometry in the data independent acquisition (MS[supserscript E]) mode for the HDX-MS analysis. We also used ion mobility as a second and orthogonal dimension of separation to overcome the spectral crowdedness. Peroxiredoxins are ubiquitous antioxidant enzymes present in many organisms. Their catalytic activity is regulated by redox dependent oligomerization and their sensitivity to overoxidation is related to the flexibility of the active site loop to undergo partial unfolding. In this research we conducted HDX-MS experiments for determining to what extent the flexibility of the active site loop governs the sensitivity of peroxiredoxins to overoxidation. As example of a robust peroxiredoxin we studied initially the conformational properties of Salmonella typhimurium AhpC wild-type protein by HDX-MS. Subsequently, we conducted comparative HDX-MS analysis on the reduced form of the wild-type protein, and two single point mutants, T77V, and T77I, with the objective to decipher to what extent the stability of the dimer-dimer (A)interface affects the conformational dynamics of the active site loop. Differential HDX-MS results of the wild-type, disulfide reduced wild-type protein have exhibited a decrease in the motility of the active site loop and the C-terminal end of the protein upon disulfide reduction. The Thr77 single point mutation by valine enhanced the dimer-dimer interaction thereby stabilizing the decamer interface and increasing the motility of the active site loop. Whereas, the substitution of T77 by isoleucine increased the motility of the interfacial region which forms the dimer-dimer interface thereby promoting the dissociation of the decamer to dimers. A technically more advanced HDX-MS experimental setup was used to study the exchange-in properties of two robust peroxiredoxins, namely the wild-type StAhpC and the C46S mutant of StAhpC, which mimicks the reduced wild-type StAhpC, in comparison to human Prx2, a peroxiredoxin which is considered as sensitive to overoxidation. When differential deuterium uptake of wild-type StAhpC, C46S mutant StAhpC were compared, increased conformational rigidity was observed in the C46S mutant protein compared to the wild-type Prx. The peptide with highest deuterium incorporation levels in the human Prx2 is much lower compared to the bacterial wild type and C46S mutant Prxs. These comparative HDX-MS studies have fostered our understanding of the underlying conformational dynamics that lead to robust and sensitive Prxs. The second protein system that was studied was a representative of the Cullin Ring Ligases (CRLs), the largest family of RING-type E3 ligases that catalyze ubiquitylation of substrates. Protein ubiquitination is a post-translational modification that regulates several important biological processes in eukaryotic cells. It involves a three enzyme enzymatic cascade consisting of an ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligases (E3). In this study focus was directed toward the Cullin scaffold protein, which adopts an elongated structure that allows substrate receptor binding at the N-terminal domain (NTD) via adaptor proteins. Its C-terminal domain (CTD) binds to E2-ubiquitin through the RBX ring subdomain. Covalent attachment of the ubiquitin-like protein Nedd8 to the conserved lysine residue of the CTD stimulates the transfer of ubiquitin to substrate proteins thereby promoting ubiquitination. The HDX-MS studies of CUL1-RBX1 protein and its neddylated form highlighted that neddylation induces significant flexibility in the conformational dynamics of the CUL1 and RBX1 protein. The HDX-MS results support a mechanistic model in which conformational flexibility in the C-terminal domain of CUL1 and a concomitant opening of the RBX1 protein is necessary to allow the ubiquitin-bound E2 to be placed in close proximity to the protein substrates thereby facilitating the CRL activity.
Book Synopsis Probing Functional Protein Dynamics Through Native-state Hydrogen Exchange Mass Spectrometry by : Maxum Paul
Download or read book Probing Functional Protein Dynamics Through Native-state Hydrogen Exchange Mass Spectrometry written by Maxum Paul and published by . This book was released on 2018 with total page 132 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis From Solution Into the Gas Phase by : Robert Gordon McAllister
Download or read book From Solution Into the Gas Phase written by Robert Gordon McAllister and published by . This book was released on 2015 with total page 198 pages. Available in PDF, EPUB and Kindle. Book excerpt: Here, we apply molecular dynamics (MD) simulations to investigate fundamental aspects of structural mass spectrometry (MS). We first examine microscopic phenomena underlying hydrogen/deuterium exchange (HDX). HDX interrogates structural dynamics of proteins by measuring the rate of Deuterium uptake into backbone amides. We perform microsecond MD simulations on ubiquitin to investigate this process. We find that HDX protection often cannot be explained by H‐bonding or solvent accessibility considerations. These findings caution against non-critical use of HDX data in structural contexts. We next use MD to examine the Electrospray ionization (ESI) mechanism of proteins. ESI is a soft ionization technique resulting in the production of gaseous protein ions. The mechanism of ion formation from nanometer sized droplets is unclear. We apply a trajectory stitching MD approach to simulate protein-containing nanodroplets, finding that natively‐folded proteins remain solvated as droplets shrink. Residual charge carriers remain following desolvation, consistent with Dole's charged residue model.
Book Synopsis Hydrogen Exchange Mass Spectrometry for Studying Protein-ligand Interactions by : Modupeola A. Sowole
Download or read book Hydrogen Exchange Mass Spectrometry for Studying Protein-ligand Interactions written by Modupeola A. Sowole and published by . This book was released on 2015 with total page 354 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen deuterium exchange (HDX) coupled with mass spectrometry is widely used for probing protein structure and dynamics. Protein-ligand interactions usually induce a reduction in the measured HDX rates an effect that may be ascribed to stabilization of the protein structure. This work aims to improve the general understanding of the changes in HDX patterns associated with ligand binding. We initially applied HDX for studying differences between oxy -hemoglobin (Oxy- Hb) and aquomet-hemoglobin (Chapter 2). The results show that the and subunits respond differently to the oxy to aquomet transition with the heme binding pocket being destabilized in both cases. The results suggest that enhanced structural dynamics in the heme binding pocket may have adverse effects on heme-protein interactions. Chapter 3 focuses on the different scenarios that can be encountered in an HDX experiment upon ligand binding. Myoglobin and hemoglobin were used as model systems, focusing on the oxy and deoxy states of both proteins. Our results demons trate that ligand binding can be stabilizing or destabilizing, leading to decreased or increased HDX rates respectively. In Chapters 4 HDX was used to probe the changes in structural dynamics of caseinolytic protease P (ClpP), an antibiotic drug target, after binding ADEP antibiotics. The mechanism of ADEP binding and the N-terminal structure of ClpP is not well understood with conflicting x-ray structures reported in literature. Our findings demonstrate that the N- terminus of ClpP remains quite unstructured after ADEP binding, while belt region undergoes tightening. Pin 1, a peptidyl prolyl isomerase, binding to a cyclic peptide inhibitor was studied in Chapter 5. Characterization of Pin1-CRYPEVEIC interactions by ot her techniques has been difficult. This study demonstrates that binding of the inhibitor triggers an overall stabilization of Pin 1. We identify a loop that interacts with basic sites of the ligand and that becomes destabilized upon ligand binding. This destabilization is ascribed to steric clashes between the peptide inhibitor and the protein.
Book Synopsis Efficient Sampling of Protein Conformational Dynamics and Prediction of Mutation Effects by : Hongbin Wan
Download or read book Efficient Sampling of Protein Conformational Dynamics and Prediction of Mutation Effects written by Hongbin Wan and published by . This book was released on 2019 with total page 166 pages. Available in PDF, EPUB and Kindle. Book excerpt: Molecular dynamics (MD) simulation is a powerful tool enabling researchers to gain insight into biological processes at the atomic level. There have been many advancements in both hardware and software in the last decade to both accelerate MD simulations and increase their predictive accuracy; however, MD simulations are typically limited to the microsecond timescale, whereas biological motions can take seconds or longer. Because of this, it remains extremely challenging to restrain simulations using ensemble-averaged experimental observables. Among various approaches to elucidate the kinetics of molecular simulations, Markov State Models (MSMs) have proven their ability to extract both kinetic and thermodynamic properties of long-timescale motions using ensembles of shorter MD simulation trajectories. In this dissertation, we have implemented an MSM path-entropy method, based on the idea of maximum-caliber, to efficiently predict the changes in protein folding behavior upon mutation. Next, we explore the accuracy of different MSM estimators applied to trajectory data obtained by adaptive seeding, in which new rounds of short MD simulations are collected from states of interest, and propose a simple method to build accurate models by population re-weighting of the transition count matrix. Finally, we explore ways to reconcile simulated ensembles with Hydrogen/Deuterium exchange (HDX) protection measurements, by constructing multi-ensemble Markov State Models (MEMMs) from biased MD simulations, and reconciling these predictions against the experimental data using the BICePs (Bayesian Inference of Conformational Populations) algorithm. We apply this approach to model the native-state conformational ensemble of apomyoglobin at neutral pH.
Book Synopsis Investigating Protein-carbohydrate Interactions with Hydrogen/deuterium Exchange Mass Spectrometry (HDX-MS) by : Jingjing Zhang
Download or read book Investigating Protein-carbohydrate Interactions with Hydrogen/deuterium Exchange Mass Spectrometry (HDX-MS) written by Jingjing Zhang and published by . This book was released on 2014 with total page 7 pages. Available in PDF, EPUB and Kindle. Book excerpt: The application of hydrogen/deuterium exchange mass spectrometry (HDX-MS) to investigating protein-carbohydrate interactions is described. Proteins from three bacterial toxins, the B subunit homopentamers of Cholera toxin (CTB5) and Shiga toxin type 1 (Stx1B5) and a fragment of Clostridium difficile toxin A (TcdA-A2), and their interactions with native carbohydrate receptors, GM1 pentasaccharide (GM1-os), Pk trisaccharide and CD-grease, respectively, were first served as model systems for this study. The results suggested that HDX-MS can serve as a useful tool for localizing the ligand binding sites in carbohydrate-binding proteins. Following this, HDX-MS measurements were applied to explore the existence of distinct HMOs binding sites on toxins. Altogether, two toxins were studied, CTB5 and TcdA-A2, and their interactions with HMOs, 2'-fucosyllactose (2'-FL) and lacto-N-tetraose (LNT), respectively. For CTB5 and its interaction with 2'-FL, a novel binding site was localized for 2'-FL, different from the one for native receptor GM1-os. For TcdA-A2 and its interaction with LNT, however, the localized binding site was the same as its native carbohydrate receptor CD-grease. A HDX-MS based titration method Protein-Ligand Interactions in solution by Mass Spectrometry, Titration and hydrogen/deuterium Exchange (PLIMSTEX), was also applied to CTB5 and its interactions GM1-os, to test the reliability of using peptides as indicators to obtain the protein-carbohydrate binding affinities. The average apparent association constant measured for the addition of GM1-os to CTB at pH 7.0 and 20 °C was found to be (1.6 ± 0.2) * 106 M-1. This is in reasonable agreement with the reported value of (3.2 ± 0.2) * 106 M-1, which was measured using direct ESI-MS assay at pH 6.9 and room temperature.
Book Synopsis Application of Hydrogen Deuterium Exchange Mass Spectrometry in Protein-ligand and Protein-protein Interactions by : Siqi Guan
Download or read book Application of Hydrogen Deuterium Exchange Mass Spectrometry in Protein-ligand and Protein-protein Interactions written by Siqi Guan and published by . This book was released on 2016 with total page 322 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteins are not static objects. They have a great variety of internal motions with different amplitudes and different timescales. These internal motions play an important role in catalytic processes. Therefore, the existence of an intimate relationship between protein dynamics and protein function is widely accepted. Due to the significance of protein dynamics, techniques have been developed to study protein dynamics including nuclear magnetic resonance (NMR) spectroscopy, electron paramagnetic resonance (EPR) spectroscopy, and mass spectrometry (MS). Compared with NMR and EPR spectroscopy, MS has less stringent sample requirements, including protein concentration and protein size. Moreover, the mass accuracy, sensitivity, and faster data analysis also have contributed to the rapid growth of MS based techniques. Hydrogen-deuterium exchange mass spectrometry (HDX-MS), a combination of HPLC and MS, has become a common and sensitive tool to probe protein structural flexibility and solution dynamics. In this dissertation, HDX-MS was applied to study dynamic changes of proteins due to substrate binding and protein-protein interactions. The GT-A glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis (MtGpgS) catalyzes the first step of biosynthesis of 6-O-methylglucose lipopolysaccharides (MGLPs), which are essential to growth and existence of mycobacterium. The HDX-MS data revealed that the two substrates UDP-glucose (UDPG) and 3-phosphoglycerate (3PGA) can bind to MtGpgS independently, disagreeing with the previous proposal that 3PGA can only bind to MtGpgS after UDPG. Moreover, 3PGA was found to bind to or allosterically affect the UDPG binding site. Furthermore, the HDX-MS data revealed that MtGpgS may provide a necessary conformation for UDPG binding, while it goes through a large conformational change on 3PGA binding. The GT-B glycosyltransferase MshA from Corynebacterium glutamicum (CgMshA) catalyzes the initial step of mycothiol biosynthesis. A large conformational change was observed in CgMshA on nucleotide binding by superimposing APO structure of CgMshA and complex structure with UDP. HDX-MS was utilized to study conformational changes of CgMshA on substrate binding from the aspect of dynamics, providing a complementary to static structures. The HDX-MS data showed that both substrates uridine diphosphate glucose-N-acetylglucosamine (UDP-GlcNAc) and 1-L-myo-inositol-1-phosphate (I1P) can bind to CgMshA independently, but the I1P binding is not productive since it binds to an uncorrect site. Moreover, the I1P binding can lead to dynamic changes of CgMshA, while only UDP-GlcNAc can induce the major conformational change of CgMshA. Furthermore, the 3PGA binding cannot induce further dynamic changes of CgMshA in the presence of UDP. HDX-MS was also employed to study dynamic changes of protein complex SufBC2D from Escherichia coli on ADP/Mg2+ binding. This complex is responsible for Fe-S cluster assembly under oxidative stress. The crystal structure of SufBC2D complex has been determined, while little dynamic information is known. So HDX-MS was applied to study dynamic changes of the SufBC2D complex. The HDX-MS data revealed that SufC has a significant conformational change, which may be required by ATP binding and hydrolysis. Moreover, SufB and SufD are detected to have dynamic changes due to SufC conformational changes. These dynamic changes suggest that SufB-SufD protomer may have a conformational change in order to provide a suitable conformation for Fe-S cluster assembly. This work demonstrates that HDX-MS can be effectively used to study protein-ligand and protein-protein interactions, as well as the accompanying changes in structural dynamics. HDX-MS data detects substrate binding mechanism and conformational changes that are not available through x-ray crystallography. With these advantages, HDX-MS has been applied in study of protein structure and dynamics, studying protein-ligand and protein-protein interactions, protein folding, as well as protein therapeutics discovery and development.
Book Synopsis Hydrogen Deuterium Exchange Mass Spectrometry for Protein-protein Interaction and Structural Dynamics by : Harsimran Singh
Download or read book Hydrogen Deuterium Exchange Mass Spectrometry for Protein-protein Interaction and Structural Dynamics written by Harsimran Singh and published by . This book was released on 2013 with total page 159 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen deuterium exchange mass spectrometry has emerged as an important technique to probe protein structure and conformational dynamics. The rate of exchange of hydrogen with deuterium by the peptide backbone is dependent on the solvent accessibility, extent of hydrogen bonding in secondary structural elements and protein dynamics. The extent and the rate of deuterium incorporation are affected by changes in protein structure, interaction with ligand, protein-protein interaction and environmental factors such as pH and temperature. These conformational changes can be global and/or local. The increase in the mass is used to localize the deuterium incorporation after pepsin digestion of the protein and analysis by electrospray ionization mass spectrometry. In this dissertation traditional HDX-MS and a new deuterium trapping assay were used to probe the interaction sites between E. coli cysteine desulfurase SufS and acceptor protein SufE. SufS and SufE form an important part of the SUF pathway, essential for the biosynthesis of Fe-S clusters under oxidative stress and iron depletion conditions. In addition, SufE is known to stimulate SufS cysteine desulfurase activity, but the mechanism is unknown. The HDX-MS results show that the regions affected by the SufS-SufE interaction are dependent on the catalytic intermediate states of the two proteins. HDX-MS was also used to probe the conformational changes resulting upon persulfuration of SufS of Cys364 in the active site. The persulfuration of SufS not only affected regions in the active site cavity, but also had other conformational changes in more distal regions. Based on our findings a model for the interaction SufS and SufE was proposed. A mechanism for the enhancement of SufS cysteine desulfurase activity upon interaction with SufE was also postulated. In all this work demonstrates that hydrogen deuterium exchange mass spectrometry and the deuterium trapping methodology optimized for this system can be easily and effectively used to study the protein-protein interactions and the accompanying changes in structural dynamics for other proteins. Deuterium trapping was demonstrated to be fast, sensitive and reliable method to deduce the changes in solvent accessibility between two or more states of a protein. Both techniques can easily be applied to large number of protein complexes to determine the regions of interaction as well as gain mechanistic information not available through traditional methods such as X-ray crystallography and NMR.
Book Synopsis Mass Spectrometry of Protein Interactions by : Kevin Downard
Download or read book Mass Spectrometry of Protein Interactions written by Kevin Downard and published by Wiley-Interscience. This book was released on 2007-08-10 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The authoritative guide to analyzing protein interactions by mass spectrometry Mass spectrometry (MS) is playing an increasingly important role in the study of protein interactions. Mass Spectrometry of Protein Interactionspresents timely and definitive discussions of the diverse range of approaches for studying protein interactions by mass spectrometry with an extensive set of references to the primary literature. Each chapter is written by authors or teams of authors who are international authorities in their fields. This leading reference text: * Discusses the direct detection of protein interactions through electrospray ionization (ESI-MS); ion mobility analysis; and matrix-assisted laser desorption/ionization (MALDI-MS) * Covers the indirect analysis of protein interactions through hydrogen-deuterium exchange (HX-MS); limited proteolysis; cross-linking; and radial probe (RP-MS) * Guides researchers in the use of mass spectrometry in structural biology, biochemistry, and protein science to map and define the huge number and diversity of protein interactions * Reviews the latest discoveries and applications and addresses new and ongoing challenges This is a comprehensive reference for researchers in academia and industry engaged in studies of protein interactions and an excellent text for graduate and postgraduate students.
Book Synopsis Mass Spectrometry-based Strategies for Protein Biophysics by : Yining Huang
Download or read book Mass Spectrometry-based Strategies for Protein Biophysics written by Yining Huang and published by . This book was released on 2016 with total page 193 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mass spectrometry (MS) is an essential tool to study proteins whose structures are of great importance in biological systems. The primary structures of proteins can be determined by the powerful sequencing capabilities of MS. The recent advancements in instrumentation and methodology have made MS increasingly valuable in probing secondary, tertiary and quaternary structures, as well as binding strength, interfaces and in solution dynamics of proteins and protein complexes. Various protein footprinting techniques, including hydrogen-deuterium exchange (HDX) and fast photochemical oxidation of proteins (FPOP), encode structural information onto the protein molecule in different forms of modifications, and then MS is utilized to interpret the mass shifts resulted from modifications and extract the structural information. Protein footprinting coupled with bottom-up proteomics, which utilizes front-end LC separation and tandem mass spectrometry, has gained a solid ground in protein biophysics. On the other hand, opportunities emerge as native MS, ion-mobility separation, gas-phase activation and fragmentation techniques allow new approaches to be developed. In the first part of this dissertation, we describe epitope mapping of three malaria antigens (Plasmodium vivax Duffy binding protein in Chapter 2, Plasmodium vivax and falciparum cell-traversal protein for ookinetes and sporozoites in Chapter 6) and one flavivirus antigen (West Nile virus envelope protein domain III (DIII) in Chapter 4) by HDX in combination with bottom-up MS. We also report epitope mapping of DIII antigen by FPOP (Chapter 5). Challenged by highly disulfide-linked antigens, sample complexity and discontinuous epitopes with only a few residues each, we implemented immunoprecipitation, non-canonical quenching and digestion protocols to achieve complete sequence coverage and map the epitopes with high confidence and spatial resolution. In the second part (Chapter 3), we describe the usage of native MS and ion mobility to characterize antigen-antibody complexes formed by the Duffy binding protein antigen with various antibodies targeting different epitopes. The last part (chapter 7 and 8) describes the development an on-line HDX, native-spray platform in conjunction with top-down MS. The strategy is validated by determining the amide hydrogen exchange rates of a model peptide at the residue level. With evidence for adequate mixing efficiency, high sequence coverage, low hydrogen scrambling and capable data analysis, we applied the platform to study solution-phase amyloid beta 1-40 monomer structure by continuous-labeling and monitoring exchange kinetics and to probe the dimerization interfaces of human insulin by pulse-labeling experiment. These seven studies demonstrate the applications of the mature bottom-up and promising top-down MS on characterizing protein conformation and protein-protein interactions.
Book Synopsis Applying Hydrogen Exchange Mass Spectrometry Coupled with Numerical Simulations to Investigate Toxic Misfolding of Beta2-microglobulin by : Angelika Hirsch
Download or read book Applying Hydrogen Exchange Mass Spectrometry Coupled with Numerical Simulations to Investigate Toxic Misfolding of Beta2-microglobulin written by Angelika Hirsch and published by . This book was released on 2019 with total page 60 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Protein Folding Protocols by : Yawen Bai
Download or read book Protein Folding Protocols written by Yawen Bai and published by Springer Science & Business Media. This book was released on 2008-02-04 with total page 332 pages. Available in PDF, EPUB and Kindle. Book excerpt: Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences.
Book Synopsis Numerical Simulations to Harness the Power of Hydrogen Exchange Mass Spectrometry in the Study of Protein Folding Landscapes by : Alexis Jaramillo
Download or read book Numerical Simulations to Harness the Power of Hydrogen Exchange Mass Spectrometry in the Study of Protein Folding Landscapes written by Alexis Jaramillo and published by . This book was released on 2012 with total page 120 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Investigating Proteome Organization and Protein Dynamics by Cross-linking Mass Spectrometry by : Julius Fürsch
Download or read book Investigating Proteome Organization and Protein Dynamics by Cross-linking Mass Spectrometry written by Julius Fürsch and published by . This book was released on 2020 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt:
