Protein Folding and Misfolding (Record no. 102037)

000 -LEADER
fixed length control field 04375nam a22005055i 4500
001 - CONTROL NUMBER
control field 978-3-642-22230-6
003 - CONTROL NUMBER IDENTIFIER
control field DE-He213
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20140220083259.0
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
fixed length control field cr nn 008mamaa
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 110915s2012 gw | s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9783642222306
-- 978-3-642-22230-6
024 7# - OTHER STANDARD IDENTIFIER
Standard number or code 10.1007/978-3-642-22230-6
Source of number or code doi
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number QH505
072 #7 - SUBJECT CATEGORY CODE
Subject category code PHVN
Source bicssc
072 #7 - SUBJECT CATEGORY CODE
Subject category code PHVD
Source bicssc
072 #7 - SUBJECT CATEGORY CODE
Subject category code SCI009000
Source bisacsh
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 571.4
Edition number 23
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Fabian, Heinz.
Relator term editor.
245 10 - TITLE STATEMENT
Title Protein Folding and Misfolding
Medium [electronic resource] :
Remainder of title Shining Light by Infrared Spectroscopy /
Statement of responsibility, etc edited by Heinz Fabian, Dieter Naumann.
264 #1 -
-- Berlin, Heidelberg :
-- Springer Berlin Heidelberg,
-- 2012.
300 ## - PHYSICAL DESCRIPTION
Extent XVI, 244 p.
Other physical details online resource.
336 ## -
-- text
-- txt
-- rdacontent
337 ## -
-- computer
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-- rdamedia
338 ## -
-- online resource
-- cr
-- rdacarrier
347 ## -
-- text file
-- PDF
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490 1# - SERIES STATEMENT
Series statement Biological and Medical Physics, Biomedical Engineering,
International Standard Serial Number 1618-7210
505 0# - FORMATTED CONTENTS NOTE
Formatted contents note Reconstruction 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 ## - SUMMARY, ETC.
Summary, etc 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.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Physics.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Biochemistry.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Biomaterials.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Physics.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Biophysics and Biological Physics.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Protein Structure.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Atomic/Molecular Structure and Spectra.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Biomaterials.
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Naumann, Dieter.
Relator term editor.
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element SpringerLink (Online service)
773 0# - HOST ITEM ENTRY
Title Springer eBooks
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Display text Printed edition:
International Standard Book Number 9783642222290
830 #0 - SERIES ADDED ENTRY--UNIFORM TITLE
Uniform title Biological and Medical Physics, Biomedical Engineering,
-- 1618-7210
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://dx.doi.org/10.1007/978-3-642-22230-6
912 ## -
-- ZDB-2-PHA

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