Protein Folding and Misfolding: Shining Light by Infrared SpectroscopyHeinz Fabian, Dieter Naumann Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems. |
Contents
Linked Landscapes and Conformational Conversions How Proteins Fold and Misfold
| 1 |
A Quantitative Reconstruction of the Amide I Contour in the IR Spectra of Peptides and Proteins From Structure to Spectrum
| 17 |
MillisecondtoMinute Protein FoldingMisfolding Events Monitored by FTIR Spectroscopy
| 53 |
Watching Dynamical Events in Protein Folding in the Time Domain from Submilliseconds to Seconds ContinuousFlow RapidMixing Infrared Spectr... | 91 |
HighPressure Vibrational Spectroscopy Studies of the Folding Misfolding and Amyloidogenesis of Proteins
| 117 |
Dynamics of Helix and Sheet Formation Studied by LaserInduced TemperatureJump IR Spectroscopy
| 147 |
Other editions - View all
Protein Folding and Misfolding: Shining Light by Infrared Spectroscopy Heinz Fabian,Dieter Naumann No preview available - 2013 |
Protein Folding and Misfolding: Shining Light by Infrared Spectroscopy Heinz Fabian,Dieter Naumann No preview available - 2011 |
Protein Folding and Misfolding: Shining Light by Infrared Spectroscopy Heinz Fabian,Dieter Naumann No preview available - 2011 |
Common terms and phrases
2DIR absorption Acad aggregation amide I band amide I contour amide I mode amide I0 amino acid amyloid fibrils angle antiparallel sheet apoMb atoms azobenzene band component Biochemistry Biol Biophys buffer caged sulfate calculated cell chain Chem conformation coordinates coupling crosspeaks denaturation diagonal difference spectra dynamics energy equilibrium experimental experiments Fabian folding and misfolding formation FTIR spectra FTIR spectroscopy hairpin helices helix hydrogen bond hydrophobic infrared spectroscopy initial intensity interaction force constant intermediate isotope labeling matrix mechanism method mixing molecular molecule native Natl Naumann negative bands observed obtained oscillators peak peptide groups photolysis Phys polypeptide pressure probe Proc protein folding protons pulse random coil reaction refolding region residues S.E. Radford sample secondary structure sheet structure simulation SNase solution solvated solvent spectrum stability stopped-flow strands Struct structural changes studies switch T-jump techniques temperature tertiary structure thermal time-resolved timescale unfolding unlabeled vibrational Wavenumber