Journal
CHEMICAL PHYSICS LETTERS
Volume 559, Issue -, Pages 88-93Publisher
ELSEVIER
DOI: 10.1016/j.cplett.2012.12.061
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Funding
- CAPES (Rede NanoBio Tec)
- CAPES (PROCAD)
- CAPES (PNPD)
- CNPq (INCT Nano(Bio)Simes)
- CNPq (Procad-Casadinho)
- FAPERN/CNPq (Pronex)
- CNPq [304283/2010-0, 474734/2011-0]
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We estimate the residue-monomer and residue-residue interaction energies of the collagen-like peptide T3-785, whose triple helix structure is the sequence X-Y-glycine (X, Y are often the imino acids proline and hydroxyproline), considering its full X-ray diffraction crystal structure, including a hydratation layer of 111 water molecules. The computations are performed within the density functional theory (DFT) scope together with a Molecular Fractionation with Conjugate Caps (MFCC) approach. We found that the hydroxyproline and proline residues play a very important role in the stabilization of the T3-785 structure, with the arginine residue in a given peptide chain exhibiting the strongest residue-strand interaction. (c) 2013 Elsevier B.V. All rights reserved.
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