Characterization of Sml1p protein oligomerization by ESI-FTICR-MS

Tomoaki Uchiki; Vibha Gupta; Chris Dealwis; Robert Hettich

Characterization of Sml1p protein oligomerization by ESI-FTICR-MS

Tomoaki Uchiki, Vibha Gupta, Chris Dealwis, Robert Hettich

Bioanalytical Mass Spectrometry

Research output: Contribution to conference › Paper › peer-review

Abstract

The Sml1p protein oligomerization was characterized by ESI-FTICR-MS. Sml1p was expressed in E. coli BL21DE3pLys bacteria by an expression plasmid DNA encoding SML1. Using the expression plasmid DNA as a template, C17S SML1 mutant was made by a PCR based site-directed mutagenesis kit, Quikchange, and the mutant protein was expressed in the same manner. The results show that Sml1p forms oligomers through non-covalent interaction, and in non-reducing conditions, a small amount of wild type Sml1p was eluted with apparent mass of 50kD, which is close to mass of tetramer (48kD).

Original language	English
Pages	353-354
Number of pages	2
State	Published - 2002
Event	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002

Conference

Conference	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	06/2/02 → 06/6/02

Cite this

@conference{18e853b29ee043a28185a73b70dde53f,

title = "Characterization of Sml1p protein oligomerization by ESI-FTICR-MS",

abstract = "The Sml1p protein oligomerization was characterized by ESI-FTICR-MS. Sml1p was expressed in E. coli BL21DE3pLys bacteria by an expression plasmid DNA encoding SML1. Using the expression plasmid DNA as a template, C17S SML1 mutant was made by a PCR based site-directed mutagenesis kit, Quikchange, and the mutant protein was expressed in the same manner. The results show that Sml1p forms oligomers through non-covalent interaction, and in non-reducing conditions, a small amount of wild type Sml1p was eluted with apparent mass of 50kD, which is close to mass of tetramer (48kD).",

author = "Tomoaki Uchiki and Vibha Gupta and Chris Dealwis and Robert Hettich",

year = "2002",

language = "English",

pages = "353--354",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

}

TY - CONF

T1 - Characterization of Sml1p protein oligomerization by ESI-FTICR-MS

AU - Uchiki, Tomoaki

AU - Gupta, Vibha

AU - Dealwis, Chris

AU - Hettich, Robert

PY - 2002

Y1 - 2002

N2 - The Sml1p protein oligomerization was characterized by ESI-FTICR-MS. Sml1p was expressed in E. coli BL21DE3pLys bacteria by an expression plasmid DNA encoding SML1. Using the expression plasmid DNA as a template, C17S SML1 mutant was made by a PCR based site-directed mutagenesis kit, Quikchange, and the mutant protein was expressed in the same manner. The results show that Sml1p forms oligomers through non-covalent interaction, and in non-reducing conditions, a small amount of wild type Sml1p was eluted with apparent mass of 50kD, which is close to mass of tetramer (48kD).

AB - The Sml1p protein oligomerization was characterized by ESI-FTICR-MS. Sml1p was expressed in E. coli BL21DE3pLys bacteria by an expression plasmid DNA encoding SML1. Using the expression plasmid DNA as a template, C17S SML1 mutant was made by a PCR based site-directed mutagenesis kit, Quikchange, and the mutant protein was expressed in the same manner. The results show that Sml1p forms oligomers through non-covalent interaction, and in non-reducing conditions, a small amount of wild type Sml1p was eluted with apparent mass of 50kD, which is close to mass of tetramer (48kD).

UR - https://www.scopus.com/pages/publications/2442698146

M3 - Paper

AN - SCOPUS:2442698146

SP - 353

EP - 354

T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

Characterization of Sml1p protein oligomerization by ESI-FTICR-MS

Abstract

Conference

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