Two-photon circular dichroism of molecular structures simulating L-tryptophan residues in proteins with secondary structures

    Authors

    Y. Vesga; C. Diaz; M. Higgs;F. E. Hernandez

    Comments

    Authors: contact us about adding a copy of your work at [email protected]

    Abbreviated Journal Title

    Chem. Phys. Lett.

    Keywords

    DENSITY-FUNCTIONAL THEORY; AMINO-ACIDS; ABSORPTION; SPECTROSCOPY; EXCHANGE; MODEL; IR; Chemistry, Physical; Physics, Atomic, Molecular & Chemical

    Abstract

    Herein, we report on the calculation and the comparative analysis of the theoretical two-photon circular dichroism (TPCD) spectra of L-tryptophan (Trp) residues in proteins with secondary structures (alpha-helix, beta-strand and random coil) conformation, down to the far-UV region (FUV). The examination of the TPCD spectra of the different conformers in each configuration reveals distinctive fingerprints in the FUV, a dark spectral region for electronic circular dichroism (ECD). Our results show the potential of FUV-TPCD to identify and study protein structures in a region never assessed before but filled with important structural information. (C) 2014 Elsevier B.V. All rights reserved.

    Journal Title

    Chemical Physics Letters

    Volume

    601

    Publication Date

    1-1-2014

    Document Type

    Editorial Material

    Language

    English

    First Page

    6

    Last Page

    12

    WOS Identifier

    WOS:000335515200002

    ISSN

    0009-2614

    Share

    COinS
     

    Accessibility Statement

    This item was created or digitized prior to April 24, 2027, or is a reproduction of legacy media created before that date. It is preserved in its original, unmodified state specifically for research, reference, or historical recordkeeping. In accordance with the ADA Title II Final Rule, the University Libraries provides accessible versions of archival materials upon request. To request an accommodation for this item, please submit an accessibility request form.