FT-IR approaches on amyloid fibril structure

被引:110
作者
Hiramatsu, H [1 ]
Kitagawa, T [1 ]
机构
[1] Okazaki Inst Integrat Biosci, Natl Inst Nat Sci, Okazaki, Aichi 4448787, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2005年 / 1753卷 / 01期
关键词
FT-IR; amide I; isotope label; IR linear dichroism; microscope; amyloid fibril structure;
D O I
10.1016/j.bbapap.2005.07.008
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
This review treats recent achievements of Fourier-transform infrared absorption spectroscopy on protein science, especially on amyloid fibril structure. It includes the brief explanation of theoretical background, description of related techniques, and recent applications to analysis of fibril structure. Concerns to theoretical background, successful analysis of Amide I in terms of transition dipole coupling between the C=O oscillators in peptide main chain has been described. The theory enables us to estimate a content of secondary structure in a protein. Related experimental techniques such as linear dichroism measurement, application of microscope, and isotope labeling, are introduced. The linear-dichroism measurement brings direct information on molecular orientation, microscope enables to treat a well-prepared particle, and isotope-label technique allows our structural discussion with one-residue resolution. Application of IR absorption spectroscopy and related techniques on amyloid fibril structure is reviewed. The model obtained is compared with protein native structure. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:100 / 107
页数:8
相关论文
共 73 条
[1]   Isotope-edited infrared linear dichroism: Determination of amide orientational relationships [J].
Anderson, TS ;
Hellgeth, J ;
Lansbury, PT .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (28) :6540-6546
[2]  
Baldwin MA, 1999, METHOD ENZYMOL, V309, P576
[3]   AMIDE MODES AND PROTEIN CONFORMATION [J].
BANDEKAR, J .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1120 (02) :123-143
[4]   Empirical relationships between isotope-edited IR spectra and helix geometry in model peptides [J].
Barber-Armstrong, W ;
Donaldson, T ;
Wijesooriya, H ;
Silva, RAGD ;
Decatur, SM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (08) :2339-2345
[5]   Time-resolved Fourier transform infrared spectroscopic imaging [J].
Bhargava, R ;
Levin, IW .
APPLIED SPECTROSCOPY, 2003, 57 (04) :357-366
[6]   Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix [J].
Blake, C ;
Serpell, L .
STRUCTURE, 1996, 4 (08) :989-998
[7]   13C isotope labeling of hydrophobic peptides.: Origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures [J].
Brauner, JW ;
Dugan, C ;
Mendelsohn, R .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (04) :677-683
[8]   Quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: From structure to spectrum [J].
Brauner, JW ;
Flach, CR ;
Mendelsohn, R .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (01) :100-109
[9]   EXAMINATION OF THE SECONDARY STRUCTURE OF PROTEINS BY DECONVOLVED FTIR SPECTRA [J].
BYLER, DM ;
SUSI, H .
BIOPOLYMERS, 1986, 25 (03) :469-487
[10]   A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods [J].
Cai, SW ;
Singh, BR .
BIOCHEMISTRY, 2004, 43 (09) :2541-2549