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Modelling the effect of osmolytes on peptide mechanical unfolding.

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Title: Modelling the effect of osmolytes on peptide mechanical unfolding.
Authors: Pieraccini, Stefano1,2,3 stefano.pieraccini@unimi.it, Conti, Simone1, Chaurasia, Shilpi1, Sironi, Maurizio1,2,3 maurizio.sironi@unimi.it
Source: Chemical Physics Letters. Jul2013, Vol. 578, p138-143. 6p.
Subjects: Peptides, Denaturation of proteins, Molecular dynamics, Osmolality, Protein structure, Free energy (Thermodynamics)
Abstract: Highlights: [•] The mechanical unfolding of a beta-hairpin is studied in presence of osmolytes. [•] The study is performed via steered molecular dynamics and umbrella sampling. [•] Analysing free energy profiles, osmoprotectants and denaturants effects are outlined. [•] Structural insight about unfolding mechanism are disclosed. [ABSTRACT FROM AUTHOR]
Copyright of Chemical Physics Letters is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 89342410
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Modelling the effect of osmolytes on peptide mechanical unfolding.
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  Data: <searchLink fieldCode="AR" term="%22Pieraccini%2C+Stefano%22">Pieraccini, Stefano</searchLink><relatesTo>1,2,3</relatesTo><i> stefano.pieraccini@unimi.it</i><br /><searchLink fieldCode="AR" term="%22Conti%2C+Simone%22">Conti, Simone</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Chaurasia%2C+Shilpi%22">Chaurasia, Shilpi</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Sironi%2C+Maurizio%22">Sironi, Maurizio</searchLink><relatesTo>1,2,3</relatesTo><i> maurizio.sironi@unimi.it</i>
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  Data: <searchLink fieldCode="JN" term="%22Chemical+Physics+Letters%22">Chemical Physics Letters</searchLink>. Jul2013, Vol. 578, p138-143. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Osmolality%22">Osmolality</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Free+energy+%28Thermodynamics%29%22">Free energy (Thermodynamics)</searchLink>
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  Data: Highlights: [•] The mechanical unfolding of a beta-hairpin is studied in presence of osmolytes. [•] The study is performed via steered molecular dynamics and umbrella sampling. [•] Analysing free energy profiles, osmoprotectants and denaturants effects are outlined. [•] Structural insight about unfolding mechanism are disclosed. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Chemical Physics Letters is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.cplett.2013.06.008
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        Text: English
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        PageCount: 6
        StartPage: 138
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        Type: general
      – SubjectFull: Denaturation of proteins
        Type: general
      – SubjectFull: Molecular dynamics
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      – SubjectFull: Osmolality
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      – SubjectFull: Protein structure
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      – SubjectFull: Free energy (Thermodynamics)
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      – TitleFull: Modelling the effect of osmolytes on peptide mechanical unfolding.
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              Text: Jul2013
              Type: published
              Y: 2013
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