Recent applications of ATR FTIR spectroscopy and imaging to proteins

被引:259
作者
Glassford, Stefanie E. [1 ]
Byrne, Bernadette [2 ]
Kazarian, Sergei G. [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Chem Engn, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, London SW7 2AZ, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2013年 / 1834卷 / 12期
关键词
FT-IR spectroscopy; Chemical imaging; Surface-enhanced spectroscopy; Protein analysis; Total internal reflection; High throughput; ENHANCED INFRARED-ABSORPTION; SILVER ISLAND FILMS; IN-SITU; SECONDARY STRUCTURE; HIGH-THROUGHPUT; SURFACE MODIFICATION; GOLD SURFACE; AMIDE-I; ADSORPTION; SPECTRA;
D O I
10.1016/j.bbapap.2013.07.015
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Attenuated Total Reflection (ATR) Fourier Transform Infrared (FTIR) spectroscopy is a label-free, non-destructive analytical technique that can be used extensively to study a wide variety of different molecules in a range of different conditions. The aim of this review is to discuss and highlight the recent advances in the applications of ATR FTIR spectroscopic imaging to proteins. It briefly covers the basic principles of ATR FUR spectroscopy and ATR FTIR spectroscopic imaging as well as their advantages to the study of proteins compared to other techniques and other forms of FTIR spectroscopy. It will then go on to examine the advances that have been made within the field over the last several years, particularly the use of ATR FTIR spectroscopy for the understanding and development of protein interaction with surfaces. Additionally, the growing potential of Surface Enhanced Infrared Spectroscopy (SEIRAS) within this area of applications will be discussed. The review includes the applications of ATR FTIR imaging to protein crystallisation and for high-throughput studies, highlighting the future potential of the technology within the field of protein structural studies and beyond. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:2849 / 2858
页数:10
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