000 04375nam a22005055i 4500
001 978-3-642-22230-6
003 DE-He213
005 20140220083259.0
007 cr nn 008mamaa
008 110915s2012 gw | s |||| 0|eng d
020 _a9783642222306
_9978-3-642-22230-6
024 7 _a10.1007/978-3-642-22230-6
_2doi
050 4 _aQH505
072 7 _aPHVN
_2bicssc
072 7 _aPHVD
_2bicssc
072 7 _aSCI009000
_2bisacsh
082 0 4 _a571.4
_223
100 1 _aFabian, Heinz.
_eeditor.
245 1 0 _aProtein Folding and Misfolding
_h[electronic resource] :
_bShining Light by Infrared Spectroscopy /
_cedited by Heinz Fabian, Dieter Naumann.
264 1 _aBerlin, Heidelberg :
_bSpringer Berlin Heidelberg,
_c2012.
300 _aXVI, 244 p.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aBiological and Medical Physics, Biomedical Engineering,
_x1618-7210
505 0 _aReconstruction of the Amide I contour in the IR spectra of proteins: From structure to spectrum; R.Mendelsohn (USA) -- Millisecond-to-minute time-resolved protein folding/misfolding events monitored by FTIR spectroscopy; H. Fabian & D. Naumann (Germany) -- Sub-millisecond events in proteins probed by continuous-flow FTIR experiments; S. Takahashi (Japan) -- Protein folding/misfolding at high pressure probed by FTIR spectroscopy; R. Winter (Germany).-Site-specific relaxation kinetics of peptides using temperature-jump IR spectroscopy and isotopic labelling; A. Barth (Sweden), K.Hauser (Germany) -- Nanosecond-to-millisecond time-resolved nonlinear infrared spectroscopy of proteins; M. Zanni (USA) -- Light triggered peptide dynamics; W. Zinth & J. Wachtveitl (Germany) -- Dynamics of alpha helix and beta-sheet formation; K. Hauser -- Time-resolved FTIR spectroscopy of peptides; A. Peralvarez-Martin, J. E.T. Corrie, A. Barth.-High pressure vibrationals spectroscopy of folding and misfolding proteins; M. Puehse, J. Markgraf, R. Winter.
520 _aInfrared 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.
650 0 _aPhysics.
650 0 _aBiochemistry.
650 0 _aBiomaterials.
650 1 4 _aPhysics.
650 2 4 _aBiophysics and Biological Physics.
650 2 4 _aProtein Structure.
650 2 4 _aAtomic/Molecular Structure and Spectra.
650 2 4 _aBiomaterials.
700 1 _aNaumann, Dieter.
_eeditor.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9783642222290
830 0 _aBiological and Medical Physics, Biomedical Engineering,
_x1618-7210
856 4 0 _uhttp://dx.doi.org/10.1007/978-3-642-22230-6
912 _aZDB-2-PHA
999 _c102037
_d102037