Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Mark E. Ridgeway"'
Publikováno v:
Analyst
Ion mobility spectrometry/mass spectrometry (IMS/MS) is widely used to study various levels of protein structure. Here, we review the current state of affairs in tandem-trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS). Two different tTI
Autor:
Kevin Jeanne Dit Fouque, Samuel A. Miller, Khoa Pham, Natarajan V. Bhanu, Yarixa L. Cintron-Diaz, Dennys Leyva, Desmond Kaplan, Valery G. Voinov, Mark E. Ridgeway, Melvin A. Park, Benjamin A. Garcia, Francisco Fernandez-Lima
Publikováno v:
Analytical chemistry. 94(44)
Post-translational modifications (PTMs) on intact histones play a major role in regulating chromatin dynamics and influence biological processes such as DNA transcription, replication, and repair. The nature and position of each histone PTM is crucia
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32:2241-2250
Blanc's Law has served as a way to predict the mobilities of ions in mixed drift gases for over 100 years yet has remained largely unexplored using newer ion mobility spectrometry (IMS) configurations, including traveling wave and trapped IMS (TIMS)
Autor:
Samuel A. Miller, Kevin Jeanne Dit Fouque, Mark E. Ridgeway, Melvin A. Park, Francisco Fernandez-Lima
Publikováno v:
J Am Soc Mass Spectrom
Trapped ion mobility spectrometry (TIMS) when coupled with mass spectrometry (MS) offers great advantages for the separation of isobaric, isomeric and/or conformeric species. In the present work, we report the advantages of coupling TIMS with a low-c
Autor:
Yuk-Ching Tse-Dinh, Francisco Fernandez-Lima, Alyssa Garabedian, Mark E. Ridgeway, Melvin A. Park, Kevin Jeanne Dit Fouque, Fenfei Leng
Publikováno v:
Anal Chem
The structural elucidation of native macromolecular assemblies has been a subject of considerable interest in native mass spectrometry (MS), and more recently in tandem with ion mobility spectrometry (IMS-MS), for a better understanding of their bioc
Publikováno v:
Anal Chem
Glycoproteins play a central role in many biological processes including disease mechanisms. Nevertheless, because glycoproteins are heterogeneous entities, it remains unclear how glycosylation modulates the protein structure and function. Here, we a
Autor:
Mark E. Ridgeway, Melvin A. Park, Christian Bleiholder, Christopher A. Wootton, Fanny C. Liu, Alina Theisen, J. S. Raaj Vellore Winfred, Jusung Lee, Nick C. Polfer
Publikováno v:
Rapid Commun Mass Spectrom
RATIONALE Tandem-ion mobility spectrometry/mass spectrometry methods have recently gained traction for the structural characterization of proteins and protein complexes. However, ion activation techniques currently coupled with tandem-ion mobility sp
Autor:
Erin M. Panczyk, Mel Park, Mark E. Ridgeway, Christian Bleiholder, Fanny C. Liu, Dalton T. Snyder, Vicki H. Wysocki, Yu-Fu Lin
Mass spectrometry-based assays in structural biology studies typically measure either intact or digested proteins. Traditionally, there are different mass spectrometers dedicated for such measurements: those focused on the rapid analysis of small mol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4992b73fe877cd9dbc4a1023b0d3c6bc
https://doi.org/10.33774/chemrxiv-2021-qr78t
https://doi.org/10.33774/chemrxiv-2021-qr78t
Publikováno v:
Journal of the American Society for Mass Spectrometry. 30:2152-2162
Using contemporary theory for ion mobility spectrometry (IMS), gas-phase ion mobilities within a trapped ion mobility-mass spectrometer (TIMS) are not easily deduced using first principle equations due to non-linear pressure changes and consequently
Publikováno v:
TrAC Trends in Analytical Chemistry. 116:324-331
Trapped Ion Mobility Spectrometry (TIMS) is a recently developed form of ion mobility spectrometry (IMS) which is flexible in its operation and readily hybridized with mass spectrometry (MS). Prototype TIMS-MS instruments are applicable to a wide ran