Techniques of two-dimensional (2D) correlation spectroscopy useful in life science research

被引：54

作者：

Noda, Isao ^{[1
]}

机构：

[1] Univ Delaware, Dept Mat Sci & Engn, Newark, DE 19716 USA

来源：

BIOMEDICAL SPECTROSCOPY AND IMAGING | 2015年 / 4卷 / 02期

关键词：

Two-dimensional correlation spectroscopy; protein secondary structures; Pareto scaling; vector projection; codistribution analysis;

D O I：

10.3233/BSI-150105

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

Several illustrative examples are presented in this tutorial review to demonstrate the utility of 2D correlation spectroscopy, especially in life science applications. A set of IR spectra for a model protein system, which is undergoing complex thermally induced changes in the secondary structures, is analyzed by 2D correlation spectroscopy. The method of constructing 2D correlation maps from temperature-dependent IR spectra and their interpretation procedure are described. The resolution of overlapped protein IR bands by 2D correlation is demonstrated, and sequential order of spectral intensity changes is determined. Newly emerging techniques in the field, such as Pareto scaling, positive null-space projection, and 2D codistribution analysis, are discussed in some detail, in addition to the traditional application of 2D correlation spectroscopy.

引用

页码：109 / 127

页数：19

共 40 条

[1] Structure and dynamics of membrane proteins as studied by infrared spectroscopy [J].

Arrondo, JLR ;

Goñi, FM .

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1999, 72 (04) :367-405

[2] The Importance of Protonation in the Investigation of Protein Phosphorylation Using Raman Spectroscopy and Raman Optical Activity [J].

Ashton, Lorna ;

Johannessen, Christian ;

Goodacre, Royston .

ANALYTICAL CHEMISTRY, 2011, 83 (20) :7978-7983

[3] Infrared spectroscopy of proteins [J].

Barth, Andreas .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2007, 1767 (09) :1073-1101

[4] 2-DIMENSIONAL VIBRATION SPECTROSCOPY - CORRELATION OF MIDINFRARED AND NEAR-INFRARED REGIONS [J].

BARTON, FE ;

HIMMELSBACH, DS ;

DUCKWORTH, JH ;

SMITH, MJ .

APPLIED SPECTROSCOPY, 1992, 46 (03) :420-429

[5] Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS) [J].

de la Arada, Igor ;

Seiler, Christian ;

Maentele, Werner .

EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2012, 41 (11) :931-938

[6] Structural Constraints Imposed by the Conserved Fusion Peptide on the HIV-1 gp41 Epitope Recognized by the Broadly Neutralizing Antibody 2F5 [J].

de la Arada, Igor ;

Julien, Jean-Philippe ;

de la Torre, Beatriz G. ;

Huarte, Nerea ;

Andreu, David ;

Pai, Emil F. ;

Arrondo, Jose L. R. ;

Nieva, Jose L. .

JOURNAL OF PHYSICAL CHEMISTRY B, 2009, 113 (41) :13626-13637

[7] Two-dimensional IR correlation spectroscopy:: Sequential events in the unfolding process of the λ Cro-V55C repressor protein [J].

Fabian, H ;

Mantsch, HH ;

Schultz, CP .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (23) :13153-13158

[8]

Goormaghtigh E, 1994, Subcell Biochem, V23, P329

[9] THE USE AND MISUSE OF FTIR SPECTROSCOPY IN THE DETERMINATION OF PROTEIN-STRUCTURE [J].

JACKSON, M ;

MANTSCH, HH .

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1995, 30 (02) :95-120

[10] Characterization of concentration-dependent infrared spectral variations of urea aqueous solutions by principal component analysis and two-dimensional correlation spectroscopy [J].

Jung, YM ;

Czarnik-Matusewicz, B ;

Kim, SB .

JOURNAL OF PHYSICAL CHEMISTRY B, 2004, 108 (34) :13008-13014

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