Why are both ends of the polypeptide chain on the outside of proteins?

@article{Hovmller2004WhyAB,
  title={Why are both ends of the polypeptide chain on the outside of proteins?},
  author={Sven Hovm{\"o}ller and Tuping Zhou},
  journal={Proteins: Structure},
  year={2004},
  volume={55}
}
Protein folding starts before the whole polypeptide has been synthesized by the ribosome. No matter how long the polypeptide is or how intricate the fold, both ends of the chain always end up on the surface. From a topological point of view, this is surprising; one would have expected to find the starting (N‐terminal) end inside the core of the folded protein, just as in a ball of yarn. We suggest here that the reason for this apparent paradox is that the first amino acid of the emerging… 
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References

SHOWING 1-10 OF 14 REFERENCES
A deeply knotted protein structure and how it might fold
TLDR
A computer algorithm is described to detect knots in open chains that is not to viewpoint and that can define the region of the chain giving rise to the knot and characterizes knots in proteins by the number of residues that must be removed from each end to abolish the knot.
The structural basis of ribosome activity in peptide bond synthesis.
TLDR
It is established that the ribosome is a ribozyme and the catalytic properties of its all-RNA active site are addressed and the mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases.
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
TLDR
The structure of the GroEL–GroES–(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cisRing, suggesting a model for an ATP-driven folding cycle that requires a double toroid.
The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14
TLDR
The first crystal structure of a mammalian SRP protein is reported, that of the mouse SRP9/14 heterodimer, determined at 2.5 Å resolution, and the Alu binding module (Alu bm) is designated, an additional member of the family of small α/β RNA binding domains.
Deep trefoil knot implicated in RNA binding found in an archaebacterial protein
TLDR
The structure of MT1 provides a first example of barrel-like fold linked to an RNA-binding domain, suggesting an extension of TIM barrel functionality to nucleic acid binding and/or catalysis.
Principles that govern the folding of protein chains.
TLDR
In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the "Thermodynamic Hypothesis," and outlined potential avenues of current and future scientific exploration.
Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein translocon
TLDR
The 2.0 Å resolution crystal structure of the cytosolic part of pea Toc34 in complex with GDP and Mg2+.
The average atomic volume and density of proteins
The density of proteins is an important quantity. For ab initio phasing in X-ray crystallography, such as low resolution envelope techniques [1, 2], an accurate protein density is essential to get a
The N-end rule: functions, mysteries, uses.
  • A. Varshavsky
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
TLDR
The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue and is discussed, and its applications are considered.
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