Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution

doi:10.1038/s41598-017-03922-3

KMS > iHuman研究所 > 特聘教授组 > Kurt Wuthrich组

	Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution
	Gessner, Chris 1; Steinchen, Wieland 5,6; Bedard, Sabrina 3; Skinner, John J.4 ; Woods, Virgil L.1; Walsh, Thomas J.2; Bange, Gert 5,6; Pantazatos, Dionysios P.2
	2017-06-19
发表期刊	SCIENTIFIC REPORTS
ISSN	2045-2322
卷号	7
发表状态	已发表
DOI	10.1038/s41598-017-03922-3
摘要	Hydrogen-deuterium exchange (HDX) coupled with mass spectrometry (HDXMS) is a rapid and effective method for localizing and determining protein stability and dynamics. Localization is routinely limited to a peptide resolution of 5 to 20 amino acid residues. HDXMS data can contain information beyond that needed for defining protein stability at single amide resolution. Here we present a method for extracting this information from an HDX dataset to generate a HDXMS protein stability fingerprint. High resolution (HR)-HDXMS was applied to the analysis of a model protein of a spectrin tandem repeat that exemplified an intuitive stability profile based on the linkage of two triple helical repeats connected by a helical linker. The fingerprint recapitulated expected stability maximums and minimums with interesting structural features that corroborate proposed mechanisms of spectrin flexibility and elasticity. HR-HDXMS provides the unprecedented ability to accurately assess protein stability at the resolution of a single amino acid. The determination of HDX stability fingerprints may be broadly applicable in many applications for understanding protein structure and function as well as protein ligand interactions.
收录类别	SCI
语种	英语
资助项目	University of California[S97-90] ; University of California[S99-44] ; University of California[L98-30]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000403650300032
出版者	NATURE PUBLISHING GROUP
WOS关键词	ELECTRON-TRANSFER DISSOCIATION ; HYDROGEN/DEUTERIUM-EXCHANGE ; RESIDUE RESOLUTION ; PROTEIN DYNAMICS ; SPECTRIN ; MS ; STABILITY ; MECHANISM ; PEPTIDES ; REPEATS
原始文献类型	Article
通讯作者	Pantazatos, Dionysios P.
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2911
专题	iHuman研究所_特聘教授组_Kurt Wuthrich组 iHuman研究所_PI研究组_徐菲组
通讯作者	Pantazatos, Dionysios P.
作者单位	1.Indiana Univ, Dept Informat & Comp, Bloomington, IN USA 2.Weill Cornell Med, Div Infect Dis, Transplantat Oncol Infect Dis Program, 1300 York Ave, New York, NY 10065 USA 3.GlaxoSmithKline, Platform Technol & Sci, Collegeville Rd, Collegeville, PA 19426 USA 4.ShanghaiTech Univ, iHuman Inst, 99 Haike Rd, Shanghai, Peoples R China 5.Philipps Univ Marburg, Fac Chem, Hans Meerwein Str, D-35043 Marburg, Germany 6.Philipps Univ Marburg, LOEWE Ctr Synthet Microbiol, Hans Meerwein Str, D-35043 Marburg, Germany
推荐引用方式 GB/T 7714	Gessner, Chris,Steinchen, Wieland,Bedard, Sabrina,et al. Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution[J]. SCIENTIFIC REPORTS,2017,7.
APA	Gessner, Chris.,Steinchen, Wieland.,Bedard, Sabrina.,Skinner, John J..,Woods, Virgil L..,...&Pantazatos, Dionysios P..(2017).Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.SCIENTIFIC REPORTS,7.
MLA	Gessner, Chris,et al."Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution".SCIENTIFIC REPORTS 7(2017).