View in EDS

Folding behaviors of apocytochrome b 5 and its mutants: Insights from high temperature molecular dynamics simulations

Saved in:
Bibliographic Details
Title: Folding behaviors of apocytochrome b 5 and its mutants: Insights from high temperature molecular dynamics simulations
Authors: Lin, Ying-Wu1,2 linlinying@hotmail.com, Nie, Chang-Ming1, Liao, Li-Fu1
Source: Journal of Molecular Structure: THEOCHEM. Sep2009, Vol. 910 Issue 1-3, p154-162. 9p.
Subjects: Protein folding, Denaturation of proteins, Cytochrome b, Genetic mutation, High temperatures, Molecular dynamics, Hemoproteins, Carrier proteins
Abstract: Abstract: Apocytochrome b 5 (apocyt b 5) with heme removal from the heme-binding core 1, and its mutants with amino acid replaced in the hydrophobic core 2, namely apocyt b 5 Y7P, P81A and H15R/S20E, have been subjected to molecular dynamics (MD) simulation at high temperature (500K) for elucidating their folding behaviors. The early events upon thermal induced unfolding were found to be in good agreement with available experimental results, and the lowest stability of Y7P was predicted among the four apoproteins. The influences of these key residues on protein folding behavior were compared directly at an atomic level. At the same time, the influences of non-native interactions of hydrogen bonds and salt-bridges on protein stabilities were analyzed in detail. The insights from current MD simulations are valuable for understanding the apoprotein folding and the holoprotein formation in terms of heme proteins. [Copyright &y& Elsevier]
Copyright of Journal of Molecular Structure: THEOCHEM 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
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 43610099
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Folding behaviors of apocytochrome b <subscript>5</subscript> and its mutants: Insights from high temperature molecular dynamics simulations
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Lin%2C+Ying-Wu%22">Lin, Ying-Wu</searchLink><relatesTo>1,2</relatesTo><i> linlinying@hotmail.com</i><br /><searchLink fieldCode="AR" term="%22Nie%2C+Chang-Ming%22">Nie, Chang-Ming</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Liao%2C+Li-Fu%22">Liao, Li-Fu</searchLink><relatesTo>1</relatesTo>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Journal+of+Molecular+Structure%3A+THEOCHEM%22">Journal of Molecular Structure: THEOCHEM</searchLink>. Sep2009, Vol. 910 Issue 1-3, p154-162. 9p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Protein+folding%22">Protein folding</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Cytochrome+b%22">Cytochrome b</searchLink><br /><searchLink fieldCode="DE" term="%22Genetic+mutation%22">Genetic mutation</searchLink><br /><searchLink fieldCode="DE" term="%22High+temperatures%22">High temperatures</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Hemoproteins%22">Hemoproteins</searchLink><br /><searchLink fieldCode="DE" term="%22Carrier+proteins%22">Carrier proteins</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Abstract: Apocytochrome b 5 (apocyt b 5) with heme removal from the heme-binding core 1, and its mutants with amino acid replaced in the hydrophobic core 2, namely apocyt b 5 Y7P, P81A and H15R/S20E, have been subjected to molecular dynamics (MD) simulation at high temperature (500K) for elucidating their folding behaviors. The early events upon thermal induced unfolding were found to be in good agreement with available experimental results, and the lowest stability of Y7P was predicted among the four apoproteins. The influences of these key residues on protein folding behavior were compared directly at an atomic level. At the same time, the influences of non-native interactions of hydrogen bonds and salt-bridges on protein stabilities were analyzed in detail. The insights from current MD simulations are valuable for understanding the apoprotein folding and the holoprotein formation in terms of heme proteins. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Molecular Structure: THEOCHEM 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.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=43610099
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.theochem.2009.06.036
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 9
        StartPage: 154
    Subjects:
      – SubjectFull: Protein folding
        Type: general
      – SubjectFull: Denaturation of proteins
        Type: general
      – SubjectFull: Cytochrome b
        Type: general
      – SubjectFull: Genetic mutation
        Type: general
      – SubjectFull: High temperatures
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
      – SubjectFull: Hemoproteins
        Type: general
      – SubjectFull: Carrier proteins
        Type: general
    Titles:
      – TitleFull: Folding behaviors of apocytochrome b 5 and its mutants: Insights from high temperature molecular dynamics simulations
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Lin, Ying-Wu
      – PersonEntity:
          Name:
            NameFull: Nie, Chang-Ming
      – PersonEntity:
          Name:
            NameFull: Liao, Li-Fu
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 30
              M: 09
              Text: Sep2009
              Type: published
              Y: 2009
          Identifiers:
            – Type: issn-print
              Value: 01661280
          Numbering:
            – Type: volume
              Value: 910
            – Type: issue
              Value: 1-3
          Titles:
            – TitleFull: Journal of Molecular Structure: THEOCHEM
              Type: main
ResultId 1