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It has, therefore, been hypothesized that the formation of amyloids is a general property common to many polypeptide chains [7].
The morphology and molecular structure of mature amyloid fibrils have been investigated extensively in vitro as many polypeptide chains form fibrillar aggregates with cross- <img src="http://journals.plos.org/plosone/article/asset?id=info?doi/10.1371/journal.pone.0019129.e005.PNG" class= inline-graphic"/> conformation [6].
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This argues for significant residual structure in unfolded polypeptide chains of many proteins.
13, 22, 23 Collagens are triple helices of polypeptide chains held together by many hydrogen bonds.
Many downstream modification events in the life of polypeptide chains (involving longer nascent peptides) are also co-translational (Fig. 1C).
This system is involved in many cytoplasmic events, such as folding of nascent polypeptide chains, rescue of misfolded proteins and assembly and disassembly of protein complexes [ 47, 48].
Many biological functions are performed by oligomeric proteins consisting of two or more polypeptide chains.
They include both exopeptidases that act on the termini of polypeptide chains and endopeptidases that act in the interior of polypeptide chains and belong to many different protein families that are grouped into clans[ 3, 4].
T-cell receptors consist of two polypeptide chains.
Hemoglobin is a protein made up of four polypeptide chains (α1, α2, β1, and β2).
Science and technology are like the two intertwined polypeptide chains in a DNA molecule.
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