title: Two-Dimensional Infrared (2DIR) Spectroscopy of the Peptide Beta3s Folding.
abstract: Probing underlying free energy landscape, pathways, and mechanism is the key for understanding protein folding in theory and experiment. Recently time-resolved two-dimensional infrared (2DIR) with femtosecond laser pulses, has emerged as a promising tool for investigating the protein folding dynamics on faster timescales than possible by NMR. We have employed molecular dynamics simulations to compute 2DIR spectra of the folding process of a peptide, Beta3s. Simulated non-chiral and chiral 2DIR signals illustrate the variation of the spectra as the peptide conformation evolves along the free energy landscape. Chiral spectra show stronger changes than the non-chiral signals because cross peaks caused by the formation of theβ-sheet are clearly resolved. Chirality-induced 2DIR may be used to detect the folding ofβ-sheet proteins with high spectral and temporal resolution.
authors: Department of Chemistry, State University of New York at Stony Brook, Stony Brook, NY11794.
authors: Zaizhi
authors: Z
authors: Lai
authors: Nicholas K
authors: NK
authors: Preketes
authors: Jun
authors: J
authors: Jiang
authors: Shaul
authors: S
authors: Mukamel
authors: Jin
authors: J
authors: Wang
keywords: Chiral signal; Free Energy Landscape; Multidimensional Spectroscopy; Nonchiral signal; Protein Folding
references: Chem Rev. 2004 Apr;104(4):2073-98
references: 15080721
references: J Phys Chem B. 2007 Sep 20;111(37):11032-46
references: 17725341
references: J Phys Chem B. 2006 Apr 13;110(14):7545-55
references: 16599536
references: J Phys Chem A. 2005 Nov 3;109(43):9747-59
references: 16833288
references: J Phys Chem B. 2011 Apr 14;115(14):4147-59
references: 21425801
references: Curr Opin Chem Biol. 2002 Oct;6(5):682-8
references: 12413554
references: J Comput Chem. 2009 Jul 30;30(10):1545-614
references: 19444816
references: J Phys Chem B. 2010 Dec 30;114(51):17201-8
references: 21138254
references: J Chem Theory Comput. 2012 Sep 11;8(9):3257-3273
references: 23341755
references: Analyst. 2012 Apr 21;137(8):1793-9
references: 22398665
references: J Mol Biol. 1995 Sep 22;252(3):366-76
references: 7563057
references: Biopolymers. 2002;67(4-5):233-6
references: 12012436
references: Proc Natl Acad Sci U S A. 2000 Sep 26;97(20):10780-5
references: 10984515
references: Protein Sci. 1999 Apr;8(4):854-65
references: 10211831
references: J Phys Chem B. 2013 Apr 25;117(16):4661-9
references: 23448437
references: PMC Biophys. 2010 Mar 19;3(1):8
references: 20302645
references: J Phys Chem B. 1998 Apr 30;102(18):3586-616
references: 24889800
references: Angew Chem Int Ed Engl. 2007;46(42):7984-7
references: 17853520
references: J Phys Chem B. 2005 Sep 15;109(36):17025-7
references: 16853169
references: Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8868-73
references: 10908673
references: Opt Lett. 2007 Mar 15;32(6):713-5
references: 17308611
references: Phys Chem Chem Phys. 2011 Feb 14;13(6):2394-400
references: 21132201
references: Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):511-6
references: 14694192
references: J Phys Chem B. 2008 May 15;112(19):5930-7
references: 18078331
references: J Phys Chem B. 2009 Aug 13;113(32):11260-73
references: 19618902
references: Angew Chem Int Ed Engl. 2009;48(21):3750-81
references: 19415637
references: Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18934-8
references: 17146054
references: Acc Chem Res. 2008 Mar;41(3):432-41
references: 18288813
references: J Phys Chem B. 2009 Jul 2;113(26):9004-15
references: 19514729
references: J Phys Chem B. 2008 Jul 24;112(29):8701-14
references: 18590307