Isotope-labeled aspartate sidechain as a non-perturbing infrared probe: Application to investigate the dynamics of a carboxylate buried inside a protein

被引：12

作者：

Abaskharon, Rachel M. ^{[1
]}

Brown, Stephen P. ^{[1
]}

Zhang, Wenkai ^{[2
]}

Chen, Jianxin ^{[2
]}

Smith, Amos B., III ^{[1
]}

Gai, Feng ^{[1
,2
]}

机构：

[1] Univ Penn, Dept Chem, 231 South 34th St, Philadelphia, PA 19104 USA

[2] Univ Penn, Ultrafast Opt Proc Lab, 231 South 34th St, Philadelphia, PA 19104 USA

来源：

CHEMICAL PHYSICS LETTERS | 2017年 / 683卷

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

2D IR SPECTROSCOPY; DEHYDROGENASE MULTIENZYME COMPLEX; SUBUNIT-BINDING DOMAIN; ALPHA-AMINO-ACIDS; M2 PROTON CHANNEL; AMIDE-I; ASYMMETRIC-SYNTHESIS; SECONDARY STRUCTURE; 2D-IR SPECTROSCOPY; N-METHYLACETAMIDE;

D O I：

10.1016/j.cplett.2017.03.064

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Because of their negatively charged carboxylates, aspartate and glutamate are frequently found at the active or binding site of proteins. However, studying a specific carboxylate in proteins that contain multiple aspartates and/or glutamates via infrared spectroscopy is difficult due to spectral overlap. We show, herein, that isotopic-labeling of the aspartate sidechain can overcome this limitation as the resultant (COO)-C-13 asymmetric stretching vibration resides in a transparent region of the protein IR spectrum. Applicability of this site-specific vibrational probe is demonstrated by using it to assess the dynamics of an aspartate ion buried inside a small protein via two-dimensional infrared spectroscopy. (C) 2017 Elsevier B.V. All rights reserved.

引用

页码：193 / 198

页数：6

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