IDEAS home Printed from https://ideas.repec.org/a/eee/phsmap/v556y2020ics0378437120304258.html
   My bibliography  Save this article

Pinning the conformation of a protein (CorA) in a solute matrix with selective binding

Author

Listed:
  • Rangubpit, Warin
  • Kitjaruwankul, Sunan
  • Sompornpisut, Pornthep
  • Pandey, R.B.

Abstract

Conformation of a protein (CorA) is examined in a matrix with mobile solute constituents as a function of solute–residue interaction strength (f) by a coarse-grained model with a Monte Carlo simulation. Solute particles are found to reach their targeted residue due to their unique interactions with the residues. Degree of slowing down of the protein depends on the interaction strength f. Unlike a predictable dependence of the radius of gyration of the same protein on interaction in an effective medium, it does not show a systematic dependence on interaction due to pinning caused by the solute binding. Spread of the protein chain is quantified by estimating its effective dimension (D) from scaling of the structure factor. Even with a lower solute–residue interaction, the protein chain appears to conform to a random-coil conformation (D∼2) in its native phase where it is globular in absence of such solute environment. The structural spread at small length scale differs from that at large scale in presence of stronger interactions: D∼2.3 at smaller length scale and D∼1.4 on larger scale with f = 3.5 while D∼1.4 at smaller length scale and D∼2.5 at larger length scales with f = 4.0.

Suggested Citation

  • Rangubpit, Warin & Kitjaruwankul, Sunan & Sompornpisut, Pornthep & Pandey, R.B., 2020. "Pinning the conformation of a protein (CorA) in a solute matrix with selective binding," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 556(C).
  • Handle: RePEc:eee:phsmap:v:556:y:2020:i:c:s0378437120304258
    DOI: 10.1016/j.physa.2020.124823
    as

    Download full text from publisher

    File URL: http://www.sciencedirect.com/science/article/pii/S0378437120304258
    Download Restriction: Full text for ScienceDirect subscribers only. Journal offers the option of making the article available online on Science direct for a fee of $3,000

    File URL: https://libkey.io/10.1016/j.physa.2020.124823?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    References listed on IDEAS

    as
    1. Kitjaruwankul, Sunan & Boonamnaj, Panisak & Paudel, Sunita Subedi & Jetsadawisut, Warin & Sompornpisut, Pornthep & Pandey, R.B., 2018. "Thermal-induced folding and unfolding of a transmembrane protein (CorA)," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 506(C), pages 987-992.
    2. Olivier Dalmas & Pornthep Sompornpisut & Francisco Bezanilla & Eduardo Perozo, 2014. "Molecular mechanism of Mg2+-dependent gating in CorA," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Louis Tung Faat Lai & Jayashree Balaraman & Fei Zhou & Doreen Matthies, 2023. "Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Ming Li & Yang Li & Yue Lu & Jianhui Li & Xuhang Lu & Yue Ren & Tianlei Wen & Yaojie Wang & Shenghai Chang & Xing Zhang & Xue Yang & Yuequan Shen, 2023. "Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:eee:phsmap:v:556:y:2020:i:c:s0378437120304258. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Catherine Liu (email available below). General contact details of provider: http://www.journals.elsevier.com/physica-a-statistical-mechpplications/ .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.