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Rod‐Coil Globular Structures – Simple Models for Proteins
Author(s) -
Nowak Christian,
Rostiashvili Vakhtang G.,
Vilgis Thomas A.
Publication year - 2005
Publication title -
macromolecular chemistry and physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.57
H-Index - 112
eISSN - 1521-3935
pISSN - 1022-1352
DOI - 10.1002/macp.200400127
Subject(s) - zigzag , electromagnetic coil , series (stratigraphy) , simple (philosophy) , representation (politics) , crystallography , line (geometry) , bar (unit) , globular protein , copolymer , helix (gastropod) , globular cluster , physics , chemistry , polymer , geometry , mathematics , nuclear magnetic resonance , quantum mechanics , politics , philosophy , galaxy , snail , law , ecology , biology , epistemology , political science , paleontology , meteorology
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.