{"title":"The early development and application of FTIR difference spectroscopy to membrane proteins: A personal perspective","authors":"K. Rothschild","doi":"10.3233/BSI-160148","DOIUrl":null,"url":null,"abstract":"Membrane proteins facilitate some of the most important cellular processes including energy conversion, ion trans- port and signal transduction. While conventional infrared absorption provides information about membrane protein secondary structure, a major challenge is to develop a dynamic picture of the functioning of membrane proteins at the molecular level. The introduction of FTIR difference spectroscopy around 1980 to study structural changes in membrane proteins along with a number of associated techniques including protein isotope labeling, site-directed mutagenesis, polarization dichroism, atten- uated total reflection and time-resolved spectroscopy have led to significant progress towards this goal. It is now possible to routinely detect conformational changes of individual amino acid residues, backbone peptides, binding ligands, chromophores and even internal water molecules under physiological conditions with time-resolution down to nanoseconds. The advent of ultrafast pulsed-IR lasers has pushed this time-resolution down to femtoseconds. The early development of FTIR difference spectroscopy as applied to membrane proteins with special focus on bacteriorhodopsin is reviewed from a personal perspective.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":null,"pages":null},"PeriodicalIF":0.3000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160148","citationCount":"19","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomedical Spectroscopy and Imaging","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3233/BSI-160148","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"SPECTROSCOPY","Score":null,"Total":0}
引用次数: 19
Abstract
Membrane proteins facilitate some of the most important cellular processes including energy conversion, ion trans- port and signal transduction. While conventional infrared absorption provides information about membrane protein secondary structure, a major challenge is to develop a dynamic picture of the functioning of membrane proteins at the molecular level. The introduction of FTIR difference spectroscopy around 1980 to study structural changes in membrane proteins along with a number of associated techniques including protein isotope labeling, site-directed mutagenesis, polarization dichroism, atten- uated total reflection and time-resolved spectroscopy have led to significant progress towards this goal. It is now possible to routinely detect conformational changes of individual amino acid residues, backbone peptides, binding ligands, chromophores and even internal water molecules under physiological conditions with time-resolution down to nanoseconds. The advent of ultrafast pulsed-IR lasers has pushed this time-resolution down to femtoseconds. The early development of FTIR difference spectroscopy as applied to membrane proteins with special focus on bacteriorhodopsin is reviewed from a personal perspective.
期刊介绍:
Biomedical Spectroscopy and Imaging (BSI) is a multidisciplinary journal devoted to the timely publication of basic and applied research that uses spectroscopic and imaging techniques in different areas of life science including biology, biochemistry, biotechnology, bionanotechnology, environmental science, food science, pharmaceutical science, physiology and medicine. Scientists are encouraged to submit their work for publication in the form of original articles, brief communications, rapid communications, reviews and mini-reviews. Techniques covered include, but are not limited, to the following: • Vibrational Spectroscopy (Infrared, Raman, Teraherz) • Circular Dichroism Spectroscopy • Magnetic Resonance Spectroscopy (NMR, ESR) • UV-vis Spectroscopy • Mössbauer Spectroscopy • X-ray Spectroscopy (Absorption, Emission, Photoelectron, Fluorescence) • Neutron Spectroscopy • Mass Spectroscopy • Fluorescence Spectroscopy • X-ray and Neutron Scattering • Differential Scanning Calorimetry • Atomic Force Microscopy • Surface Plasmon Resonance • Magnetic Resonance Imaging • X-ray Imaging • Electron Imaging • Neutron Imaging • Raman Imaging • Infrared Imaging • Terahertz Imaging • Fluorescence Imaging • Near-infrared spectroscopy.