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Exploring the Protein Folding Dynamics of Beta3s with Two‐Dimensional Ultraviolet (2DUV) Spectroscopy
Author(s) -
Lai Zaizhi,
Jiang Jun,
Mukamel Shaul,
Wang Jin
Publication year - 2014
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201300141
Subject(s) - chemistry , ultraviolet , chromophore , spectroscopy , chemical physics , protein folding , femtosecond , folding (dsp implementation) , ultraviolet visible spectroscopy , molecular dynamics , photochemistry , computational chemistry , laser , optoelectronics , optics , physics , biochemistry , electrical engineering , organic chemistry , quantum mechanics , engineering
Ultraviolet (UV) spectra of proteins originate from electronic excitations of their backbone chromophore and aromatic side chains and provide a sensitive probe of the secondary structure. Recently developed femtosecond lasers allow multidimensional spectroscopy to be extended into the UV regime. Two‐dimensional UV (2DUV) techniques, with short pulses, provide a promising tool to study the structures and dynamics of proteins. We combined 2DUV spectroscopy and molecular dynamics generated free energy profiles to simulate the protein electronic transitions and UV photon echo signals to monitor the protein folding process of the small protein Beta3s. Near‐ultraviolet (NUV) and far‐ultraviolet (FUV) signals illustrate the variation of the 2D correlation plots when the protein evolves along the underlying free energy landscape. Chiral polarization configurations of the NUV and FUV pulses are sensitive to protein structural evolution. This work provides a protocol for applying multidimensional UV spectroscopy to study protein folding.