title: Use of infrared spectroscopy to monitor protein structure and stability.
abstract: One of the most versatile methods for monitoring the structure of proteins, either in solution or in the solid state, is Fourier transform infrared spectroscopy. Also known as mid-range infrared, which covers the frequency range from 4000 to 400 cm(-1), this wavelength region includes bands that arise from three conformationally sensitive vibrations within the peptide backbone (amide I, II and III). Of these vibrations, amide I is the most widely used and can provide information on secondary structure composition and structural stability. One of the advantages of infrared spectroscopy is that it can be used with proteins that are either in solution or in the solid state. The use of infrared to monitor protein structure and stability is summarized herein. In addition, specialized infrared methods are presented, such as techniques for the study of membrane proteins and oriented samples. In addition, there is a growing body of literature on the use of infrared to follow reaction kinetics and ligand binding in proteins, as well as a number of infrared studies on protein dynamics. Finally, the potential for using near-infrared spectroscopy to study protein structure is introduced.
authors.affiliation: Legacy BioDesign LLC, 1826 Monarch Circle, Loveland, CO 80538-8773, USA. legacybiodesign@cs.com
authors.forename: Mark Cornell
authors.initials: MC
authors.lastname: Manning
mesh_terms: D000818:Animals; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013816:Thermodynamics; D014732:Vibration
chemical_list: D010455:Peptides; D011506:Proteins