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Conservation of folding pathways in evolutionarily distant globin sequences

Academic Article
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Overview

authors

  • Nishimura, C.
  • Prytulla, S.
  • Dyson, Jane
  • Wright, Peter

publication date

  • August 2000

journal

  • Nature Structural Biology  Journal

abstract

  • To test the hypothesis that the folding pathways of evolutionarily related proteins with similar three-dimensional structures but widely different sequences should be similar, the folding pathway of apoleghemoglobin has been characterized using stopped-flow circular dichroism, heteronuclear NMR pulse labeling techniques and mass spectrometry. The pathway of folding was found to differ significantly from that of a protein of the same family, apomyoglobin, although both proteins appear to fold through helical burst phase intermediates. For leghemoglobin, the burst phase intermediate exhibits stable helical structure in the G and H helices, together with a small region in the center of the E helix. The A and B helices are not stabilized until later stages of the folding process. The structure of the burst phase folding intermediate thus differs from that of apomyoglobin, in which stable helical structure is formed in the A, B, G and H helix regions.

subject areas

  • Amino Acid Sequence
  • Animals
  • Apoproteins
  • Circular Dichroism
  • Evolution, Molecular
  • Globins
  • Hemeproteins
  • Hydrogen-Ion Concentration
  • Kinetics
  • Leghemoglobin
  • Mass Spectrometry
  • Microscopy, Fluorescence
  • Models, Molecular
  • Molecular Sequence Data
  • Myoglobin
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Denaturation
  • Protein Folding
  • Protein Renaturation
  • Protein Structure, Secondary
  • Sequence Alignment
  • Thermodynamics
  • Urea
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Identity

International Standard Serial Number (ISSN)

  • 1072-8368

Digital Object Identifier (DOI)

  • 10.1038/77985

PubMed ID

  • 10932254
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Additional Document Info

start page

  • 679

end page

  • 686

volume

  • 7

issue

  • 8

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