ACS Measurement Science Au最新文献_第2页

Optimizing Solid Microneedle Design: A Comprehensive ML-Augmented DOE Approach 优化固体微针设计：综合 ML 增强 DOE 方法

ACS Measurement Science Au Pub Date : 2024-08-06 DOI: 10.1021/acsmeasuresciau.4c00021

Ahmed Choukri Abdullah, Erfan Ahmadinejad, Savas Tasoglu

{"title":"Optimizing Solid Microneedle Design: A Comprehensive ML-Augmented DOE Approach","authors":"Ahmed Choukri Abdullah, Erfan Ahmadinejad, Savas Tasoglu","doi":"10.1021/acsmeasuresciau.4c00021","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00021","url":null,"abstract":"Microneedles (MNs), that is, a matrix of micrometer-scale needles, have diverse applications in drug delivery, skincare therapy, and health monitoring. MNs offer a minimally invasive alternative to hypodermic needles, characterized by rapid and painless procedures, cost-effective fabrication methods, and reduced tissue damage. This study explores four MN designs, cone-shaped, tapered cone-shaped, pyramidal with a square base, and pyramidal with a triangular-shaped base, and their optimization based on predefined criteria. The workflow encompasses three loading conditions: compressive load during insertion, critical buckling load, and bending loading resulting from incorrect insertion. Geometric parameters such as base radius/width, tip radius/width, height, and tapered angle tip influence the output criteria, namely, total deformation, critical buckling loads, factor of safety (FOS), and bending stress. The comprehensive framework employing a design of experiment approach within the ANSYS workbench toolbox establishes a mathematical model and a response surface fitting model. The resulting regression model, sensitivity chart, and response curve are used to create a multiobjective optimization problem that helps achieve an optimized MN geometrical design across the introduced four shapes, integrating machine learning (ML) techniques. This study contributes valuable insights into a potential ML-augmented optimization framework for MNs via needle designs to stay durable for various physiologically relevant conditions.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141931242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cross-Species Applications of Peptide Substrate Reporters to Quantitative Measurements of Kinase Activity 多肽底物报告器在激酶活性定量测量中的跨物种应用

ACS Measurement Science Au Pub Date : 2024-08-02 DOI: 10.1021/acsmeasuresciau.4c00030

Mengqi Jonathan Fan, Misha Mehra, Kunwei Yang, Rahuljeet S. Chadha, Sababa Anber, Michelle L. Kovarik

{"title":"Cross-Species Applications of Peptide Substrate Reporters to Quantitative Measurements of Kinase Activity","authors":"Mengqi Jonathan Fan, Misha Mehra, Kunwei Yang, Rahuljeet S. Chadha, Sababa Anber, Michelle L. Kovarik","doi":"10.1021/acsmeasuresciau.4c00030","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00030","url":null,"abstract":"Peptide substrate reporters are short chains of amino acids designed to act as substrates for enzymes of interest. Combined with capillary electrophoresis and laser-induced fluorescence detection (CE-LIF), they are powerful molecular tools for quantitative measurements of enzyme activity even at the level of single cells. Although most peptide substrate reporters have been optimized for human or murine cells in health-related applications, their performance in nonmammalian organisms remains largely unexplored. In this study, we evaluated three peptide substrate reporters for protein kinase B (PKB) in two eukaryotic microbes, Dictyostelium discoideum and Tetrahymena thermophila, which are evolutionarily distant from mammals and from each other yet express PKB homologues. All three peptide substrate reporters were phosphorylated in lysates from both organisms but with varying phosphorylation kinetics and stability. To demonstrate reporter utility, we used one to screen for and identify the previously unknown stimulus needed to activate PHK5, the PKB homologue in T. thermophila. In D. discoideum, we employed the highly quantitative nature of these assays using CE-LIF to make precise measurements of PKB activity in response to transient stimulation, drug treatment, and genetic mutation. These results underscore the broad applicability of peptide substrate reporters across diverse species while highlighting the need for further research to determine effective peptide stabilization strategies across different biological contexts.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"44 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-08-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141881272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Waveform Optimization for the In Vitro Detection of Caffeic Acid by Fast-Scan Cyclic Voltammetry 快速扫描循环伏安法体外检测咖啡酸的波形优化

ACS Measurement Science Au Pub Date : 2024-07-31 DOI: 10.1021/acsmeasuresciau.4c00029

Joseph N. Tonn, Richard B. Keithley

{"title":"Waveform Optimization for the In Vitro Detection of Caffeic Acid by Fast-Scan Cyclic Voltammetry","authors":"Joseph N. Tonn, Richard B. Keithley","doi":"10.1021/acsmeasuresciau.4c00029","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00029","url":null,"abstract":"Caffeic acid is a polyphenol of critical importance in plants, involved in a variety of physiological processes including lignin formation, cellular growth, stress response, and external signaling. This small molecule also acts as a powerful antioxidant and thus has therapeutic potential for a variety of health conditions. Traditional methods of detecting caffeic acid lack appropriate temporal resolution to monitor real time concentration changes on a subsecond time scale with nM detection limits. Here we report on the first usage of fast-scan cyclic voltammetry with carbon fiber microelectrodes for the detection of caffeic acid. Through the use of flow injection analysis, the optimal waveform for its detection under acidic conditions at a scan rate of 400 V/s was determined to be sawtooth-shaped, from 0 to 1.4 to −0.4 to 0 V. Signal was linear with concentration up to 1 μM with a sensitivity of 44.8 ± 1.3 nA/μM and a detection limit of 2.3 ± 0.2 nM. The stability of its detection was exceptional, with an average of 0.96% relative standard deviation across 32 consecutive injections. This waveform was also successful in detecting other catechol-based plant antioxidants including 5-chlorogenic acid, oleuropein, rosmarinic acid, chicoric acid, and caffeic acid phenethyl ester. Finally, we show the successful use of fast-scan cyclic voltammetry in monitoring the degradation of caffeic acid by polyphenol oxidase on a subsecond time scale via a novel modification of a Ramsson cell. This work demonstrates that fast-scan cyclic voltammetry can be used to successfully monitor real-time dynamic changes in the concentrations of catechol-containing plant polyphenols.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"38 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141867838","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Scanning Gas Diffusion Electrode Setup for Real-Time Analysis of Catalyst Layers 用于实时分析催化剂层的扫描气体扩散电极装置

ACS Measurement Science Au Pub Date : 2024-07-12 DOI: 10.1021/acsmeasuresciau.4c00018

Ina Reichmann, Vicent Lloret, Konrad Ehelebe, Pascal Lauf, Ken Jenewein, Karl J. J. Mayrhofer, Serhiy Cherevko

{"title":"Scanning Gas Diffusion Electrode Setup for Real-Time Analysis of Catalyst Layers","authors":"Ina Reichmann, Vicent Lloret, Konrad Ehelebe, Pascal Lauf, Ken Jenewein, Karl J. J. Mayrhofer, Serhiy Cherevko","doi":"10.1021/acsmeasuresciau.4c00018","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00018","url":null,"abstract":"The scanning gas diffusion electrode (S-GDE) half-cell is introduced as a new tool to improve the evaluation of electrodes used in electrochemical energy conversion technologies. It allows both fast screening and fundamental studies of real catalyst layers by applying coupled mass spectrometry techniques such as inductively coupled plasma mass spectrometry and online gas mass spectrometry. Hence, the proposed setup overcomes the limitations of aqueous model systems and full cell-level studies, bridging the gap between the two approaches. In this proof-of-concept work, standard fuel cell electrodes are investigated at elevated oxygen reduction reaction current densities, while dissolved Ptx+ ions in the electrolyte and gaseous CO2 in the outlet gas stream are detected to track platinum dissolution and carbon corrosion, respectively. Relevant current densities of up to 0.75 A cm–2 are demonstrated. The electrochemically active surface area, oxygen reduction reaction activity, and Pt dissolution rates are quantified and benchmarked to the values obtained in the conventional stationary GDE half-cell. Moreover, it is found that Pt dissolution is suppressed when O2 is purged into the catalyst layer. Overall, this work demonstrates the feasibility of fast fuel cell electrode screening obtaining, complementary to electrochemical, mass spectrometry data necessary in fundamental studies on structure/performance relationships under actual reaction conditions. While Pt/C, in relevance to its fuel cell application, is used in this study, the proposed setup can be applied in water electrolysis, CO2 conversion, metal-air batteries, and other neighbor technologies.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"5 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-07-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141610731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Impedimetric Measurement of Exchange Currents and Ionic Diffusion Coefficients in Individual Pseudocapacitive Nanoparticles 单个伪电容纳米粒子中交换电流和离子扩散系数的浸渍测量法

ACS Measurement Science Au Pub Date : 2024-07-11 DOI: 10.1021/acsmeasuresciau.4c00017

Brian Roehrich, Lior Sepunaru

{"title":"Impedimetric Measurement of Exchange Currents and Ionic Diffusion Coefficients in Individual Pseudocapacitive Nanoparticles","authors":"Brian Roehrich, Lior Sepunaru","doi":"10.1021/acsmeasuresciau.4c00017","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00017","url":null,"abstract":"Among electroanalytical techniques, electrochemical impedance spectroscopy (EIS) offers the unique advantage of a high degree of frequency resolution. This enables EIS to readily deconvolute between the capacitive, resistive, and diffusional processes that underlie electrochemical devices. Here, we report the measurement of impedance spectra of individual, pseudocapacitive nanoparticles. We chose Prussian blue as our model system, as it couples an electron-transfer reaction with sodium ion intercalation─processes which, while intrinsically convoluted, can be readily resolved using EIS. We used a scanning electrochemical cell microscope (SECCM) to isolate single Prussian blue particles in a microdroplet and measured their impedance spectra using the multi-sine, fast Fourier transform technique. In doing so, we were able to extract the exchange current density and sodium ion diffusivity for each particle, which respectively inform on their electronic and ionic conductivities. Surprisingly, these parameters vary by over an order of magnitude between particles and are not correlated to particle size nor to each other. The implication of this apparent heterogeneity is that in a hypothetical battery cathode, one active particle may transfer electrons 10 times faster than its neighbor; another may suffer from sluggish sodium ion transport and have restricted charging rate capabilities compared to a better-performing particle elsewhere in the same electrode. Our results inform on this intrinsic heterogeneity while demonstrating the utility of EIS in future single-particle studies.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"46 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Impedimetric Measurement of Exchange Currents and Ionic Diffusion Coefficients in Individual Pseudocapacitive Nanoparticles 单个伪电容纳米粒子中交换电流和离子扩散系数的浸渍测量法

IF 4.6

ACS Measurement Science Au Pub Date : 2024-07-11 DOI: 10.1021/acsmeasuresciau.4c0001710.1021/acsmeasuresciau.4c00017

Brian Roehrich, and , Lior Sepunaru*,

{"title":"Impedimetric Measurement of Exchange Currents and Ionic Diffusion Coefficients in Individual Pseudocapacitive Nanoparticles","authors":"Brian Roehrich,  and , Lior Sepunaru*, ","doi":"10.1021/acsmeasuresciau.4c0001710.1021/acsmeasuresciau.4c00017","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00017https://doi.org/10.1021/acsmeasuresciau.4c00017","url":null,"abstract":"Among electroanalytical techniques, electrochemical impedance spectroscopy (EIS) offers the unique advantage of a high degree of frequency resolution. This enables EIS to readily deconvolute between the capacitive, resistive, and diffusional processes that underlie electrochemical devices. Here, we report the measurement of impedance spectra of individual, pseudocapacitive nanoparticles. We chose Prussian blue as our model system, as it couples an electron-transfer reaction with sodium ion intercalation─processes which, while intrinsically convoluted, can be readily resolved using EIS. We used a scanning electrochemical cell microscope (SECCM) to isolate single Prussian blue particles in a microdroplet and measured their impedance spectra using the multi-sine, fast Fourier transform technique. In doing so, we were able to extract the exchange current density and sodium ion diffusivity for each particle, which respectively inform on their electronic and ionic conductivities. Surprisingly, these parameters vary by over an order of magnitude between particles and are not correlated to particle size nor to each other. The implication of this apparent heterogeneity is that in a hypothetical battery cathode, one active particle may transfer electrons 10 times faster than its neighbor; another may suffer from sluggish sodium ion transport and have restricted charging rate capabilities compared to a better-performing particle elsewhere in the same electrode. Our results inform on this intrinsic heterogeneity while demonstrating the utility of EIS in future single-particle studies.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"4 4","pages":"467–474 467–474"},"PeriodicalIF":4.6,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acsmeasuresciau.4c00017","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142010399","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

MALDI Mass Spectrometry on High-Density Droplet Arrays: Matrix Deposition, Selective Removal, and Recrystallization 高密度液滴阵列上的 MALDI 质谱分析：基质沉积、选择性去除和重结晶

ACS Measurement Science Au Pub Date : 2024-07-05 DOI: 10.1021/acsmeasuresciau.4c00016

Simon F. Berlanda, Maximilian Breitfeld, Petra S. Dittrich

{"title":"MALDI Mass Spectrometry on High-Density Droplet Arrays: Matrix Deposition, Selective Removal, and Recrystallization","authors":"Simon F. Berlanda, Maximilian Breitfeld, Petra S. Dittrich","doi":"10.1021/acsmeasuresciau.4c00016","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.4c00016","url":null,"abstract":"High-density droplet arrays are emerging as a powerful tool for high-throughput bioanalytical applications. These arrays are formed of thousands of nanoliter droplets, which can be analyzed by various optical and spectroscopic methods as well as label-free matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). However, special precautions are required for the massive number of small droplets, particularly in the deposition of matrix compounds. Here, we introduce a new workflow for the analytical preparation of an array comprising 6048 droplets, which significantly improves the intensity of the MALDI-MS signals. We deposited matrix compounds in a custom-made sublimation chamber followed by a recrystallization step to achieve significant signal intensity increases for three model proteins with low, medium, and large masses, respectively. Furthermore, selective removal of the matrix before recrystallization enhanced the spatial resolution and increased the signal intensity by an average of 57%. This method can be easily standardized and upscaled for the preparation of an even larger number of droplets per array for MS analysis.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"40 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141552741","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry 利用质谱技术进行自下而上蛋白质组学研究的全面概述

ACS Measurement Science Au Pub Date : 2024-06-04 DOI: 10.1021/acsmeasuresciau.3c00068

Yuming Jiang, Devasahayam Arokia Balaya Rex, Dina Schuster, Benjamin A. Neely, Germán L. Rosano, Norbert Volkmar, Amanda Momenzadeh, Trenton M. Peters-Clarke, Susan B. Egbert, Simion Kreimer, Emma H. Doud, Oliver M. Crook, Amit Kumar Yadav, Muralidharan Vanuopadath, Adrian D. Hegeman, Martín L. Mayta, Anna G. Duboff, Nicholas M. Riley, Robert L. Moritz, Jesse G. Meyer

{"title":"Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry","authors":"Yuming Jiang, Devasahayam Arokia Balaya Rex, Dina Schuster, Benjamin A. Neely, Germán L. Rosano, Norbert Volkmar, Amanda Momenzadeh, Trenton M. Peters-Clarke, Susan B. Egbert, Simion Kreimer, Emma H. Doud, Oliver M. Crook, Amit Kumar Yadav, Muralidharan Vanuopadath, Adrian D. Hegeman, Martín L. Mayta, Anna G. Duboff, Nicholas M. Riley, Robert L. Moritz, Jesse G. Meyer","doi":"10.1021/acsmeasuresciau.3c00068","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.3c00068","url":null,"abstract":"Proteomics is the large scale study of protein structure and function from biological systems through protein identification and quantification. “Shotgun proteomics” or “bottom-up proteomics” is the prevailing strategy, in which proteins are hydrolyzed into peptides that are analyzed by mass spectrometry. Proteomics studies can be applied to diverse studies ranging from simple protein identification to studies of proteoforms, protein-protein interactions, protein structural alterations, absolute and relative protein quantification, post-translational modifications, and protein stability. To enable this range of different experiments, there are diverse strategies for proteome analysis. The nuances of how proteomic workflows differ may be challenging to understand for new practitioners. Here, we provide a comprehensive overview of different proteomics methods. We cover from biochemistry basics and protein extraction to biological interpretation and orthogonal validation. We expect this Review will serve as a handbook for researchers who are new to the field of bottom-up proteomics.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"30 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141257711","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry 利用质谱技术进行自下而上蛋白质组学研究的全面概述

IF 4.6

ACS Measurement Science Au Pub Date : 2024-06-04 DOI: 10.1021/acsmeasuresciau.3c0006810.1021/acsmeasuresciau.3c00068

Yuming Jiang, Devasahayam Arokia Balaya Rex, Dina Schuster, Benjamin A. Neely, Germán L. Rosano, Norbert Volkmar, Amanda Momenzadeh, Trenton M. Peters-Clarke, Susan B. Egbert, Simion Kreimer, Emma H. Doud, Oliver M. Crook, Amit Kumar Yadav, Muralidharan Vanuopadath, Adrian D. Hegeman, Martín L. Mayta, Anna G. Duboff, Nicholas M. Riley, Robert L. Moritz and Jesse G. Meyer*,

{"title":"Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry","authors":"Yuming Jiang, Devasahayam Arokia Balaya Rex, Dina Schuster, Benjamin A. Neely, Germán L. Rosano, Norbert Volkmar, Amanda Momenzadeh, Trenton M. Peters-Clarke, Susan B. Egbert, Simion Kreimer, Emma H. Doud, Oliver M. Crook, Amit Kumar Yadav, Muralidharan Vanuopadath, Adrian D. Hegeman, Martín L. Mayta, Anna G. Duboff, Nicholas M. Riley, Robert L. Moritz and Jesse G. Meyer*, ","doi":"10.1021/acsmeasuresciau.3c0006810.1021/acsmeasuresciau.3c00068","DOIUrl":"https://doi.org/10.1021/acsmeasuresciau.3c00068https://doi.org/10.1021/acsmeasuresciau.3c00068","url":null,"abstract":"Proteomics is the large scale study of protein structure and function from biological systems through protein identification and quantification. “Shotgun proteomics” or “bottom-up proteomics” is the prevailing strategy, in which proteins are hydrolyzed into peptides that are analyzed by mass spectrometry. Proteomics studies can be applied to diverse studies ranging from simple protein identification to studies of proteoforms, protein-protein interactions, protein structural alterations, absolute and relative protein quantification, post-translational modifications, and protein stability. To enable this range of different experiments, there are diverse strategies for proteome analysis. The nuances of how proteomic workflows differ may be challenging to understand for new practitioners. Here, we provide a comprehensive overview of different proteomics methods. We cover from biochemistry basics and protein extraction to biological interpretation and orthogonal validation. We expect this Review will serve as a handbook for researchers who are new to the field of bottom-up proteomics.","PeriodicalId":29800,"journal":{"name":"ACS Measurement Science Au","volume":"4 4","pages":"338–417 338–417"},"PeriodicalIF":4.6,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acsmeasuresciau.3c00068","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142010488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Underestimation of the Complexity of Kd Determination: Causes, Implications, and Ways to Improve 低估 Kd 测定的复杂性：原因、影响和改进方法

ACS Measurement Science Au Pub Date : 2024-05-22 DOI: 10.1021/acsmeasuresciau.4c00023

Sergey N. Krylov*,

引用次数: 0