alexa Surface FTIR Techniques to Analyze the Conformation of
ISSN: 2161-0398

Journal of Physical Chemistry & Biophysics
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Review Article

Surface FTIR Techniques to Analyze the Conformation of Proteins/ Peptides in H2O Environment

Joseph D Combs, Cuauhtemoc U Gonzalez and Chengshan Wang*
Chemistry Department, Middle Tennessee State University, Murfreesboro, TN 37132, United States of America
Corresponding Author : Chengshan Wang
Chemistry Department, Middle Tennessee State University
Murfreesboro, TN 37132, United States of America
Tel: 6156929167
E-mail: [email protected]
Received: January 18, 2016 Accepted: February 05, 2016 Published: February 09, 2016
Citation: Combs JD, Gonzalez CU, Wang C (2016) Surface FTIR Techniques to Analyze the Conformation of Proteins/Peptides in H2O Environment. J Phys Chem Biophys 6:202. doi:10.4172/2161-0398.1000202
Copyright: © 2016 Combs JD, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 

Abstract

Proteins/peptides, which are involved in various biochemical processes in biological systems, contain infrared (IR) active vibrations. Among all the IR absorption bands of proteins/peptides, the amide I band arises mainly from the stretching vibration of the carbonyls (C=O) in backbone amide bonds and is sensitive to the conformations (such as α– helix, β–sheet, unstructured conformation, and so on) in a protein/peptide. Therefore, the amide I band has been used to monitor the biophysical/biochemical behavior of proteins/peptides in biological samples (e.g., living cells or tissues). However, obtaining reproducible IR spectra of proteins/peptides in H2O solution was challenging by direct transmission measurement using a liquid cell with milli-meter level path length, due to the intensive IR absorption of H2O around 1620 cm-1 which overlaps the amide I band. Thus, lots of the IR spectra of proteins/peptides were accomplished in D2O, which has IR absorption around 1200 cm-1. Since D2O may not be a favorable solvent for biological samples, the position of the amide I band of various conformations was needed as a reference for biological samples. Consequently, various surface FTIR techniques (such as Infrared Reflection-Absorption Spectroscopy or IRRAS, and Attenuated Total Reflection or ATR) have been developed to obtain the IR spectra of proteins/peptides in H2O environment and have been reviewed here.

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