What vibrations tell us about proteins.
This review deals with current concepts of vibrational spectroscopy for the investigation of protein structure and function. While the focus is on infrared (IR) spectroscopy, some of the general aspects also apply to Raman spectroscopy. Special emphasis is on the amide I vibration of the polypeptide backbone that is used for secondary-structure analysis. Theoretical as well as experimental aspects are covered including transition dipole coupling. Further topics are discussed, namely the absorption of amino-acid side-chains, 1H/2H exchange to study the conformational flexibility and reaction-induced difference spectroscopy for the investigation of reaction mechanisms with a focus on interpretation tools.
Barth
Andreas
A
Institut für Biophysik, Johann Wolfgang Goethe-Universität, Theodor Stern-Kai 7, Haus 74, D-60590 Frankfurt am Main, Germany. Andreas.Barth@dbb.su.se
Zscherp
Christian
C
D000577:Amides / Q000737:chemistry*; D007259:Infrared Rays; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000528:radiation effects; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013059:Spectrum Analysis, Raman / Q000379:methods*; D013329:Structure-Activity Relationship; D014732:Vibration
D000577:Amides; D011506:Proteins