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Proc Natl Acad Sci U S A. Feb 1978; 75(2): 559–563.
PMCID: PMC411294

Respective roles of short- and long-range interactions in protein folding.

Abstract

A lattice model of protein is studied by a Monte Carlo simulation method. The native conformation of the lattice protein molecule is stabilized by specific long-range and short-ranged interactions. By comparing results of simulation for different relative weights of the long- and short-range interactions, it is concluded that the specific long-range interactions are essential for highly cooperative stabilization of the native conformation and that the short-range interactions accelerate the folding and unfolding transitions.

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Selected References

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  • Epand RM, Scheraga HA. The influence of long-range interactions on the structure of myoglobin. Biochemistry. 1968 Aug;7(8):2864–2872. [PubMed]
  • Anfinsen CB. The formation and stabilization of protein structure. Biochem J. 1972 Jul;128(4):737–749. [PMC free article] [PubMed]
  • Taketomi H, Ueda Y, Gō N. Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions. Int J Pept Protein Res. 1975;7(6):445–459. [PubMed]

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