TY - JOUR
T1 - FT-IR approaches on amyloid fibril structure
AU - Hiramatsu, Hirotsugu
AU - Kitagawa, Teizo
PY - 2005/11/10
Y1 - 2005/11/10
N2 - 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 CO 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.
AB - 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 CO 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.
KW - Amide I
KW - Amyloid fibril structure
KW - FT-IR
KW - IR linear dichroism
KW - Isotope label
KW - Microscope
UR - http://www.scopus.com/inward/record.url?scp=27744577906&partnerID=8YFLogxK
U2 - 10.1016/j.bbapap.2005.07.008
DO - 10.1016/j.bbapap.2005.07.008
M3 - Article
C2 - 16084779
AN - SCOPUS:27744577906
VL - 1753
SP - 100
EP - 107
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -