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Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides.

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Title: Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides.
Authors: Lin, Yu-Fu1 (AUTHOR), Yousef, Enas N.1 (AUTHOR), Torres, Efren1 (AUTHOR), Truong, Linh1 (AUTHOR), Zahnow, James M.1 (AUTHOR), Donald, Cole B.1 (AUTHOR), Qin, Ying1 (AUTHOR), Angel, Laurence A.1 (AUTHOR) Laurence.Angel@tamuc.edu
Source: Journal of the American Society for Mass Spectrometry. Oct2019, Vol. 30 Issue 10, p2068-2081. 14p.
Subjects: Histidine, Tertiary structure, Zinc-finger proteins, Cysteine, Amino acid sequence, Zinc ions
Abstract: Zinc fingers are proteins that are characterized by the coordination of zinc ions by an amino acid sequence that commonly contains two histidines and two cysteines (2His-2Cys motif). Investigations of oligopeptides that contain the 2His-2Cys motif, e.g., acetyl-His1-Cys2-Gly3-Pro4-Tyr5-His6-Cys7, have discovered they exhibit pH-dependent Zn(II) chelation and have redox activities with Cu(I/II), forming a variety of metal complexes. To further understand how these 2His-2Cys oligopeptides bind these metal ions, we have undertaken a series of ion mobility–mass spectrometry and B3LYP/LanL2DZ computational studies of structurally related heptapeptides. Starting with the sequence above, we have modified the potential His, Cys, or C-terminus binding sites and report how these changes in primary structure affect the oligopeptides positive and negative charge states, conformational structure, collision-induced breakdown energies, and how effectively Zn(II) binds to these sequences. The results show evidence that the weak acid-base properties of Cys-His are intrinsically linked and can result in an intramolecular salt-bridged network that affects the oligopeptide properties. [ABSTRACT FROM AUTHOR]
Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society 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: 139274624
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PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides.
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  Data: <searchLink fieldCode="AR" term="%22Lin%2C+Yu-Fu%22">Lin, Yu-Fu</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Yousef%2C+Enas+N%2E%22">Yousef, Enas N.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Torres%2C+Efren%22">Torres, Efren</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Truong%2C+Linh%22">Truong, Linh</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zahnow%2C+James+M%2E%22">Zahnow, James M.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Donald%2C+Cole+B%2E%22">Donald, Cole B.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Qin%2C+Ying%22">Qin, Ying</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Angel%2C+Laurence+A%2E%22">Angel, Laurence A.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> Laurence.Angel@tamuc.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+the+American+Society+for+Mass+Spectrometry%22">Journal of the American Society for Mass Spectrometry</searchLink>. Oct2019, Vol. 30 Issue 10, p2068-2081. 14p.
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  Data: <searchLink fieldCode="DE" term="%22Histidine%22">Histidine</searchLink><br /><searchLink fieldCode="DE" term="%22Tertiary+structure%22">Tertiary structure</searchLink><br /><searchLink fieldCode="DE" term="%22Zinc-finger+proteins%22">Zinc-finger proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Cysteine%22">Cysteine</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+acid+sequence%22">Amino acid sequence</searchLink><br /><searchLink fieldCode="DE" term="%22Zinc+ions%22">Zinc ions</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Zinc fingers are proteins that are characterized by the coordination of zinc ions by an amino acid sequence that commonly contains two histidines and two cysteines (2His-2Cys motif). Investigations of oligopeptides that contain the 2His-2Cys motif, e.g., acetyl-His1-Cys2-Gly3-Pro4-Tyr5-His6-Cys7, have discovered they exhibit pH-dependent Zn(II) chelation and have redox activities with Cu(I/II), forming a variety of metal complexes. To further understand how these 2His-2Cys oligopeptides bind these metal ions, we have undertaken a series of ion mobility–mass spectrometry and B3LYP/LanL2DZ computational studies of structurally related heptapeptides. Starting with the sequence above, we have modified the potential His, Cys, or C-terminus binding sites and report how these changes in primary structure affect the oligopeptides positive and negative charge states, conformational structure, collision-induced breakdown energies, and how effectively Zn(II) binds to these sequences. The results show evidence that the weak acid-base properties of Cys-His are intrinsically linked and can result in an intramolecular salt-bridged network that affects the oligopeptide properties. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society 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: 10.1007/s13361-019-02275-7
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      – Code: eng
        Text: English
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        PageCount: 14
        StartPage: 2068
    Subjects:
      – SubjectFull: Histidine
        Type: general
      – SubjectFull: Tertiary structure
        Type: general
      – SubjectFull: Zinc-finger proteins
        Type: general
      – SubjectFull: Cysteine
        Type: general
      – SubjectFull: Amino acid sequence
        Type: general
      – SubjectFull: Zinc ions
        Type: general
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      – TitleFull: Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides.
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            NameFull: Lin, Yu-Fu
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            – D: 01
              M: 10
              Text: Oct2019
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              Y: 2019
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