publication . Article . Other literature type . 2004

Nature of structural inhomogeneities on folding a helix and their influence on spectral measurements

Gnanakaran, S.; Hochstrasser, Robin M.; García, Angel E.;
Open Access
  • Published: 14 Jun 2004 Journal: Proceedings of the National Academy of Sciences, volume 101, pages 9,229-9,234 (issn: 0027-8424, eissn: 1091-6490, Copyright policy)
  • Publisher: Proceedings of the National Academy of Sciences
Abstract
Extensive conformational sampling and calculations of vibrational coupling provide a quantitative basis for the structurally inhomogeneous spectra of the amide unit in aqueous solutions containing folded and unfolded state distributions of helices. Replica exchange molecular dynamics simulations of the capped helical peptide, AA(AAKAA)3AAY, is carried out over a range of temperatures, where the system populates the folded and unfolded states. This sampling defines a set of ensembles that characterizes the conformational variability for configurations identified by their fraction of helical content. The effects of hydrogen bonding, both internal and external (wit...
Subjects
arXiv: Quantitative Biology::BiomoleculesPhysics::Biological Physics
free text keywords: Denaturation (biochemistry), Spectral line, Molecular physics, Hydrogen bond, Crystallography, Helix, Chemistry, Protein folding, Alpha helix, Rotational–vibrational coupling, Molecular dynamics, Biological Sciences
Powered by OpenAIRE Open Research Graph
Any information missing or wrong?Report an Issue
publication . Article . Other literature type . 2004

Nature of structural inhomogeneities on folding a helix and their influence on spectral measurements

Gnanakaran, S.; Hochstrasser, Robin M.; García, Angel E.;