A novel microfluidic system for the rapid analysis of protein thermal stability

Xin Yang; Jia Liu; Ye Lei Xie; Yang Wang; Hong Ying; Qiong Wu; Wei Huang; Gareth Jenkins

doi:10.1039/c4an00173g

A novel microfluidic system for the rapid analysis of protein thermal stability

Xin Yang, Jia Liu, Ye Lei Xie, Yang Wang, Hong Ying, Qiong Wu, Wei Huang, Gareth Jenkins

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

We describe a simple microfluidic device for the rapid analysis of protein thermal stability using a novel imaging method. The change in UV absorption upon thermal denaturation or aggregation of proteins is used to get a spatial image of proteins' folding or aggregation state along a linear temperature gradient.

Original language	English
Pages (from-to)	2683-2686
Number of pages	4
Journal	Analyst
Volume	139
Issue number	11
DOIs	https://doi.org/10.1039/c4an00173g
State	Published - 6 May 2014
Externally published	Yes

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title = "A novel microfluidic system for the rapid analysis of protein thermal stability",

abstract = "We describe a simple microfluidic device for the rapid analysis of protein thermal stability using a novel imaging method. The change in UV absorption upon thermal denaturation or aggregation of proteins is used to get a spatial image of proteins' folding or aggregation state along a linear temperature gradient.",

author = "Xin Yang and Jia Liu and Xie, \{Ye Lei\} and Yang Wang and Hong Ying and Qiong Wu and Wei Huang and Gareth Jenkins",

year = "2014",

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T1 - A novel microfluidic system for the rapid analysis of protein thermal stability

AU - Yang, Xin

AU - Liu, Jia

AU - Xie, Ye Lei

AU - Wang, Yang

AU - Ying, Hong

AU - Wu, Qiong

AU - Huang, Wei

AU - Jenkins, Gareth

PY - 2014/5/6

Y1 - 2014/5/6

N2 - We describe a simple microfluidic device for the rapid analysis of protein thermal stability using a novel imaging method. The change in UV absorption upon thermal denaturation or aggregation of proteins is used to get a spatial image of proteins' folding or aggregation state along a linear temperature gradient.

AB - We describe a simple microfluidic device for the rapid analysis of protein thermal stability using a novel imaging method. The change in UV absorption upon thermal denaturation or aggregation of proteins is used to get a spatial image of proteins' folding or aggregation state along a linear temperature gradient.

UR - https://www.scopus.com/pages/publications/84899829135

U2 - 10.1039/c4an00173g

DO - 10.1039/c4an00173g

M3 - 文章

C2 - 24722552

AN - SCOPUS:84899829135

SN - 0003-2654

VL - 139

SP - 2683

EP - 2686

JO - Analyst

JF - Analyst

IS - 11

ER -

A novel microfluidic system for the rapid analysis of protein thermal stability

Abstract

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