Protein-Folding Landscapes in Multi-Chain Systems

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Computational studies of proteins have significantly improved our understanding of protein folding. These studies are normally carried out using chains in isolation. However, in many systems of practical interest, proteins fold in the presence of other molecules. To obtain insight into folding in such situations, we compare the thermodynamics of folding for a Miyazawa-Jernigan model 64-mer in isolation to results obtained in the presence of additional chains. The melting temperature falls as the chain concentration increases. In multi-chain systems, free-energy landscapes for folding show an increased preference for misfolded states. Misfolding is accompanied by an increase in inter-protein interactions; however, ... continued below

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Cellmer, Troy; Bratko, Dusan; Prausnitz, John M. & Blanch, Harvey June 20, 2005.

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Computational studies of proteins have significantly improved our understanding of protein folding. These studies are normally carried out using chains in isolation. However, in many systems of practical interest, proteins fold in the presence of other molecules. To obtain insight into folding in such situations, we compare the thermodynamics of folding for a Miyazawa-Jernigan model 64-mer in isolation to results obtained in the presence of additional chains. The melting temperature falls as the chain concentration increases. In multi-chain systems, free-energy landscapes for folding show an increased preference for misfolded states. Misfolding is accompanied by an increase in inter-protein interactions; however, near the folding temperature, the transition from folded chains to misfolded and associated chains isentropically driven. A majority of the most probable inter-protein contacts are also native contacts, suggesting that native topology plays a role in early stages of aggregation.

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  • Journal Name: Proceedings of National Academy of Sciences; Journal Volume: 102; Journal Issue: 33; Related Information: Journal Publication Date: 08/16/2005

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  • Report No.: LBNL--57925
  • Grant Number: DE-AC02-05CH11231
  • Office of Scientific & Technical Information Report Number: 861262
  • Archival Resource Key: ark:/67531/metadc785545

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  • June 20, 2005

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  • Dec. 3, 2015, 9:30 a.m.

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  • Dec. 16, 2016, 1:14 p.m.

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Cellmer, Troy; Bratko, Dusan; Prausnitz, John M. & Blanch, Harvey. Protein-Folding Landscapes in Multi-Chain Systems, article, June 20, 2005; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc785545/: accessed July 18, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.