Monte Carlo simulation of protein folding in the presence of residue‐specific binding sites

Rossinsky, Eddie; Srebnik, Simcha

doi:10.1002/bip.20365

Cited by 4 publications

(2 citation statements)

References 32 publications

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“…Recent years have seen significant progress in the development and application of theoretical and computational strategies for the elucidation of the mechanisms underlying MIP synthesis and ligand‐polymer recognition events, and as a tool for MIP design . The impact of these techniques is seen in the increasing frequency with which they are being used as a predictive tool in the development of new MIP systems.…”

Section: Fundamental Aspectsmentioning

confidence: 99%

Molecular imprinting science and technology: a survey of the literature for the years 2004-2011

2014

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SummaryHerein we present a survey of the literature covering the development of molecular imprinting science and technology over the years 2004 to 2011. In total, 3779 references to the original papers, reviews, edited volumes and monographs from this period are included, along with recently identified uncited materials from prior to 2004 which were omitted in the first instalment of this series covering the years 1930 to 2003. 1 In the presentation of the assembled references, a section presenting reviews and monographs covering the area is followed by sections describing fundamental aspects of molecular imprinting including the development of novel polymer formats. Thereafter, literature describing efforts to apply these polymeric materials to a range of application areas is presented. Current trends and areas of rapid development are discussed.2

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Section: Fundamental Aspectsmentioning

confidence: 99%

Molecular imprinting science and technology: a survey of the literature for the years 2004-2011

2014

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“…Moreover, MIP could also weakly bind the unfolded form in its binding site, thereby facilitating refolding through an "induced-fit" mechanism. An ensemble growth Monte Carlo simulation study on protein folding has suggested that residue-specific external binding sites enhance the fraction of the correctly folded conformation (23). The mechanism responsible for the MIPassisted refolding remains to be determined in detail.…”

Section: Refolding Of Lysozyme In the Presence Of Mipsmentioning

confidence: 99%

Molecularly Imprinted Polymer-Assisted Refolding of Lysozyme

Haruki¹,

Konnai²,

Shimada³

et al. 2007

Biotechnol. Prog.

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For production of active proteins using heterologous expression systems, refolding of proteins from inclusion bodies often creates a bottleneck due to its poor yield. In this study, we show that molecularly imprinted polymer (MIP) toward native lysozyme promotes the folding of chemically denatured lysozyme. The MIP, which was prepared with 1 M acrylamide, 1 M methacrylic acid, 1 M 2-(dimethylamino)ethyl methacrylate, and 5 mg/mL lysozyme, successfully promoted the refolding of lysozyme, whereas the non-imprinted polymer did not. The refolding yield of 90% was achieved when 15 mg of the MIP was added to 0.3 mg of the unfolded lysozyme. The parallel relationship between the refolding yield and the binding capacity of the MIP suggests that MIP promotes refolding through shifting the folding equilibrium toward the native form by binding the refolded protein.

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Charged groups synergically enhance protein imprinting in amphoteric polyacrylamide cryogels

Yang

Zhou

Liu

et al. 2016

J of Applied Polymer Sci

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Proteins are amphoteric biopolymers with unevenly charged exterior surfaces. Taking this point fully into account could accomplish ingenious recognition systems for the biological macromolecues. Molecularly imprinted polymers (MIPs) are good tools to study the interactions between polymeric matrices and template molecules. Here different protein imprinted cryogels were prepared. Imprinting factors (IFs) were determined with bovine serum albumin (BSA) as the template. The IF of the polymeric cryogel made from only acrylamide (AM) and N,N′‐methylenebisacrylamide (BisAM) is about 1.38. The introduction of charged monomers, either acrylic acid or diallylamine, would increase IFs obviously. One of the basic cryogels gave the maximum IF (about 2.0) of that type. As both acrylic acid and diallylamine were involved, IFs were further increased. An amphoteric cryogel with a suitable acid‐base ratio gave a high IF of about 3.7. Whatever used alone or both, too many added acidic or basic monomers resulted in IF reduction. Taking full advantage of charged groups in MIPs could be a good way to manipulate protein–polymer interactions. © 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 43851.

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Monte Carlo simulation of protein folding in the presence of residue‐specific binding sites

Cited by 4 publications

References 32 publications

Molecular imprinting science and technology: a survey of the literature for the years 2004-2011

Molecular imprinting science and technology: a survey of the literature for the years 2004-2011

Molecularly Imprinted Polymer-Assisted Refolding of Lysozyme

Charged groups synergically enhance protein imprinting in amphoteric polyacrylamide cryogels

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