Structure and stability of chiral beta-tapes: a computational coarse-grained approach

G  Bellesia; M V  Fedorov; Y A  Kuznetsov; E G  Timoshenko

doi:10.1063/1.1866012

Structure and stability of chiral beta-tapes: a computational coarse-grained approach

G Bellesia, M V Fedorov, Y A Kuznetsov, E G Timoshenko

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

We present two coarse-grained models of different levels of detail for the description of beta-sheet tapes obtained from equilibrium self-assembly of short rationally designed oligopeptides in solution. Here we only consider the case of the homopolymer oligopeptides with the identical sidegroups attached, in which the tapes have a helicoid surface with two equivalent sides. The influence of the chirality parameter on the geometrical characteristics, namely the diameter, interstrand distance, and pitch, of the tapes has been investigated. The two models are found to produce equivalent results suggesting a considerable degree of universality in conformations of the tapes.

Original language	English
Article number	134901
Pages (from-to)	-
Number of pages	10
Journal	Journal of Chemical Physics
Volume	122
Issue number	13
DOIs	https://doi.org/10.1063/1.1866012
Publication status	Published - 1 Apr 2005

Keywords

amphiphilic assemblies
globular proteins
energy landscape
helical ribbons
sheet peptide
folded states

Access to Document

10.1063/1.1866012

Cite this

@article{f2b846080b3f450db5809bc9b5efccaa,

title = "Structure and stability of chiral beta-tapes: a computational coarse-grained approach",

abstract = "We present two coarse-grained models of different levels of detail for the description of beta-sheet tapes obtained from equilibrium self-assembly of short rationally designed oligopeptides in solution. Here we only consider the case of the homopolymer oligopeptides with the identical sidegroups attached, in which the tapes have a helicoid surface with two equivalent sides. The influence of the chirality parameter on the geometrical characteristics, namely the diameter, interstrand distance, and pitch, of the tapes has been investigated. The two models are found to produce equivalent results suggesting a considerable degree of universality in conformations of the tapes.",

keywords = "amphiphilic assemblies, globular proteins, energy landscape, helical ribbons, sheet peptide, folded states",

author = "G Bellesia and Fedorov, {M V} and Kuznetsov, {Y A} and Timoshenko, {E G}",

year = "2005",

month = apr,

day = "1",

doi = "10.1063/1.1866012",

language = "English",

volume = "122",

pages = "--",

journal = "Journal of Chemical Physics",

issn = "0021-9606",

number = "13",

}

TY - JOUR

T1 - Structure and stability of chiral beta-tapes: a computational coarse-grained approach

AU - Bellesia, G

AU - Fedorov, M V

AU - Kuznetsov, Y A

AU - Timoshenko, E G

PY - 2005/4/1

Y1 - 2005/4/1

N2 - We present two coarse-grained models of different levels of detail for the description of beta-sheet tapes obtained from equilibrium self-assembly of short rationally designed oligopeptides in solution. Here we only consider the case of the homopolymer oligopeptides with the identical sidegroups attached, in which the tapes have a helicoid surface with two equivalent sides. The influence of the chirality parameter on the geometrical characteristics, namely the diameter, interstrand distance, and pitch, of the tapes has been investigated. The two models are found to produce equivalent results suggesting a considerable degree of universality in conformations of the tapes.

AB - We present two coarse-grained models of different levels of detail for the description of beta-sheet tapes obtained from equilibrium self-assembly of short rationally designed oligopeptides in solution. Here we only consider the case of the homopolymer oligopeptides with the identical sidegroups attached, in which the tapes have a helicoid surface with two equivalent sides. The influence of the chirality parameter on the geometrical characteristics, namely the diameter, interstrand distance, and pitch, of the tapes has been investigated. The two models are found to produce equivalent results suggesting a considerable degree of universality in conformations of the tapes.

KW - amphiphilic assemblies

KW - globular proteins

KW - energy landscape

KW - helical ribbons

KW - sheet peptide

KW - folded states

U2 - 10.1063/1.1866012

DO - 10.1063/1.1866012

M3 - Article

SN - 0021-9606

VL - 122

SP - -

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 13

M1 - 134901

ER -

Structure and stability of chiral beta-tapes: a computational coarse-grained approach

Abstract

Keywords

Access to Document

Fingerprint

Cite this