## Abstract Using computer simulations as a tool for thought experiments, we investigate the influence of the helical backbone geometry in the association process and the final structures of a simple model which mimics parallel, two‐stranded coiled‐coil proteins. We define three types of helices: t
Rod-Coil Globular Structures – Simple Models for Proteins
✍ Scribed by Christian Nowak; Vakhtang G. Rostiashvili; Thomas A. Vilgis
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 242 KB
- Volume
- 206
- Category
- Article
- ISSN
- 1022-1352
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✦ Synopsis
Abstract
Summary: In this article, we discuss the phase behavior of rod‐coil copolymers with two main methods. First, a scaling theory on different conformations is presented, which shows how micelles form. The circumstances of their stability is discussed. In the second part, we have formulated the general self‐consistent field theory (SCFT) for the rod(or helix)‐coil multiblock copolymer globule. This model and both approaches provide a simple description of the interplay between the secondary and tertiary structures in a globule α‐helix proteins.
Pictorial representation of a used series ratio: each bar, zigzag line and fat dot correspond to $\hat G_{{\rm rod}} ,;\hat G_{{\rm coil}} ,$ and σ^1/2^, respectively.
magnified imagePictorial representation of a used series ratio: each bar, zigzag line and fat dot correspond to $\hat G_{{\rm rod}} ,;\hat G_{{\rm coil}} ,$ and σ^1/2^, respectively.
📜 SIMILAR VOLUMES
Polaron models have been considered for the electron states in protein globules existing in a solvent. These models account for two fundamental effects, viz, polarization interaction of an electron with the conformational vibrations and the heterogeneity of the medium. Equations have been derived to
The three-dimensional structure of the assembly domain of the cartilage oligomeric matrix protein (COMP) has been modeled. The model demonstrates a parallel five-stranded coiled coil and fits well with a large amount of experimental data that describe the oligomerization state, the a-helical conform