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Title: Communication: Quantitative multi-site frequency maps for amide I vibrational spectroscopy

An accurate method for predicting the amide I vibrational spectrum of a given protein structure has been sought for many years. Significant progress has been made recently by sampling structures from molecular dynamics simulations and mapping local electrostatic variables onto the frequencies of individual amide bonds. Agreement with experiment, however, has remained largely qualitative. Previously, we used dipeptide fragments and isotope-labeled constructs of the protein G mimic NuG2b as experimental standards for developing and testing amide I frequency maps. Here, we combine these datasets to test different frequency-map models and develop a novel method to produce an optimized four-site potential (4P) map based on the CHARMM27 force field. Together with a charge correction for glycine residues, the optimized map accurately describes both experimental datasets, with average frequency errors of 2–3 cm{sup −1}. This 4P map is shown to be convertible to a three-site field map which provides equivalent performance, highlighting the viability of both field- and potential-based maps for amide I spectral modeling. The use of multiple sampling points for local electrostatics is found to be essential for accurate map performance.
Authors:
 [1] ;  [2] ;  [3]
  1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 (United States)
  2. (United States)
  3. Department of Chemistry, University of Chicago, Chicago, Illinois 60637 (United States)
Publication Date:
OSTI Identifier:
22493496
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Chemical Physics; Journal Volume: 143; Journal Issue: 6; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ABSORPTION SPECTROSCOPY; CORRECTIONS; ELECTROSTATICS; ERRORS; GLYCINE; MAPPING; MOLECULAR DYNAMICS METHOD; PERFORMANCE; POTENTIALS; PROTEIN STRUCTURE; PROTEINS; RESIDUES; SAMPLING; SIMULATION; VIABILITY; VIBRATIONAL STATES