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Macromolecular Crowding and Protein Stability

Wang, Yaqiang ; Sarkar, Mohona ; Smith, Austin E ; Krois, Alexander S ; Pielak, Gary J

Journal of the American Chemical Society, 2012-10, Vol.134 (40), p.16614-16618 [Periódico revisado por pares]

United States: American Chemical Society

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  • Título:
    Macromolecular Crowding and Protein Stability
  • Autor: Wang, Yaqiang ; Sarkar, Mohona ; Smith, Austin E ; Krois, Alexander S ; Pielak, Gary J
  • Assuntos: Animals ; Ficoll - chemistry ; Humans ; Macromolecular Substances - chemistry ; Muramidase - chemistry ; Povidone - chemistry ; Protein Stability ; Proteins - chemistry ; Serum Albumin, Bovine - chemistry ; Thermodynamics ; Ubiquitin - chemistry
  • É parte de: Journal of the American Chemical Society, 2012-10, Vol.134 (40), p.16614-16618
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: An understanding of cellular chemistry requires knowledge of how crowded environments affect proteins. The influence of crowding on protein stability arises from two phenomena, hard-core repulsions and soft (i.e., chemical) interactions. Most efforts to understand crowding effects on protein stability, however, focus on hard-core repulsions, which are inherently entropic and stabilizing. We assessed these phenomena by measuring the temperature dependence of NMR-detected amide proton exchange and used these data to extract the entropic and enthalpic contributions of crowding to the stability of ubiquitin. Contrary to expectations, the contribution of chemical interactions is large and in many cases dominates the contribution from hardcore repulsions. Our results show that both chemical interactions and hard-core repulsions must be considered when assessing the effects of crowding and help explain previous observations about protein stability and dynamics in cells.
  • Editor: United States: American Chemical Society
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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