Literature DB >> 18799750

Proteins with weakly funneled energy landscapes challenge the classical structure-function paradigm.

Garegin A Papoian1.   

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Year:  2008        PMID: 18799750      PMCID: PMC2567144          DOI: 10.1073/pnas.0807977105

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


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  12 in total

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3.  Sequence complexity of disordered protein.

Authors:  P Romero; Z Obradovic; X Li; E C Garner; C J Brown; A K Dunker
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4.  Tuning the heterogeneous early folding dynamics of phosphoglycerate kinase.

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5.  A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes.

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Review 6.  Fluctuating enzymes: lessons from single-molecule studies.

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7.  Structure and dynamics of a molten globular enzyme.

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8.  On the relationship between folding and chemical landscapes in enzyme catalysis.

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Journal:  J Mol Biol       Date:  2005-12-01       Impact factor: 5.469

Review 10.  Navigating the folding routes.

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  23 in total

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Review 4.  The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.

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6.  AWSEM-IDP: A Coarse-Grained Force Field for Intrinsically Disordered Proteins.

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Review 7.  Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.

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10.  Choice of Force Field for Proteins Containing Structured and Intrinsically Disordered Regions.

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Journal:  Biophys J       Date:  2020-02-29       Impact factor: 4.033

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