A diffusion–collision–adhesion model for the kinetics of myoglobin refolding View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1980-08

AUTHORS

F E Cohen, M J Sternberg, D C Phillips, I D Kuntz, P A Kollman

ABSTRACT

There are two distinct experimental and theoretical problems of protein folding: the thermodynamic issue of characterizing the folded state, and the kinetic question of the path between the unfolded and native states. Here we consider the second question and present a diffusion--collision--adhesion model for the folding of the alpha-helical protein myoglobin. In particular, we consider the fast refolding species of the unfolded state and ignore the slow transition between unfolded states that has been attributed to proline isomerization. More... »

PAGES

632-634

References to SciGraph publications

  • 1976-04. Protein-folding dynamics in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/286632a0

    DOI

    http://dx.doi.org/10.1038/286632a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1029043289

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7402344


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