Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin
Copyright © 2020 American Chemical Society. The water dynamics, as characterized by the local hydrophobicity (LH), is investigated for tetrameric hemoglobin (Hb) and dimeric melittin. For the T0 to R0 transition in Hb, it is found that LH provides additional molecular-level insight into the Perutz m...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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American Chemical Society (ACS)
2022
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| Online Access: | https://hdl.handle.net/1721.1/132583.2 |
| _version_ | 1811098259053084672 |
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| author | Pezzella, Marco El Hage, Krystel Niesen, Michiel JM Shin, Sucheol Willard, Adam P Meuwly, Markus Karplus, Martin |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Pezzella, Marco El Hage, Krystel Niesen, Michiel JM Shin, Sucheol Willard, Adam P Meuwly, Markus Karplus, Martin |
| author_sort | Pezzella, Marco |
| collection | MIT |
| description | Copyright © 2020 American Chemical Society. The water dynamics, as characterized by the local hydrophobicity (LH), is investigated for tetrameric hemoglobin (Hb) and dimeric melittin. For the T0 to R0 transition in Hb, it is found that LH provides additional molecular-level insight into the Perutz mechanism, i.e., the breaking and formation of salt bridges at the α1/β2 and α2/β1 interface is accompanied by changes in LH. For Hb in cubic water boxes with 90 and 120 Å edge length it is observed that following a decrease in LH as a consequence of reduced water density or change of water orientation at the protein/water interface the α/β interfaces are destabilized; this is a hallmark of the Perutz stereochemical model for the T to R transition in Hb. The present work thus provides a dynamical view of the classical structural model relevant to the molecular foundations of Hb function. For dimeric melittin, earlier results by Cheng and Rossky [ Nature 1998, 392, 696-699[ are confirmed and interpreted on the basis of LH from simulations in which the protein structure is frozen. For the flexible melittin dimer, the changes in the local hydration can be as much as 30% greater than for the rigid dimer, reflecting the fact that protein and water dynamics are coupled. |
| first_indexed | 2024-09-23T17:12:28Z |
| format | Article |
| id | mit-1721.1/132583.2 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T17:12:28Z |
| publishDate | 2022 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/132583.22022-07-19T20:05:45Z Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin Pezzella, Marco El Hage, Krystel Niesen, Michiel JM Shin, Sucheol Willard, Adam P Meuwly, Markus Karplus, Martin Massachusetts Institute of Technology. Department of Chemistry Copyright © 2020 American Chemical Society. The water dynamics, as characterized by the local hydrophobicity (LH), is investigated for tetrameric hemoglobin (Hb) and dimeric melittin. For the T0 to R0 transition in Hb, it is found that LH provides additional molecular-level insight into the Perutz mechanism, i.e., the breaking and formation of salt bridges at the α1/β2 and α2/β1 interface is accompanied by changes in LH. For Hb in cubic water boxes with 90 and 120 Å edge length it is observed that following a decrease in LH as a consequence of reduced water density or change of water orientation at the protein/water interface the α/β interfaces are destabilized; this is a hallmark of the Perutz stereochemical model for the T to R transition in Hb. The present work thus provides a dynamical view of the classical structural model relevant to the molecular foundations of Hb function. For dimeric melittin, earlier results by Cheng and Rossky [ Nature 1998, 392, 696-699[ are confirmed and interpreted on the basis of LH from simulations in which the protein structure is frozen. For the flexible melittin dimer, the changes in the local hydration can be as much as 30% greater than for the rigid dimer, reflecting the fact that protein and water dynamics are coupled. 2022-07-19T20:05:44Z 2021-09-20T18:23:11Z 2022-07-19T20:05:44Z 2020 2020-11-13T14:32:23Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/132583.2 en 10.1021/ACS.JPCB.0C04320 Journal of Physical Chemistry B Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/octet-stream American Chemical Society (ACS) arXiv |
| spellingShingle | Pezzella, Marco El Hage, Krystel Niesen, Michiel JM Shin, Sucheol Willard, Adam P Meuwly, Markus Karplus, Martin Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title | Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title_full | Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title_fullStr | Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title_full_unstemmed | Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title_short | Water Dynamics Around Proteins: T- and R-States of Hemoglobin and Melittin |
| title_sort | water dynamics around proteins t and r states of hemoglobin and melittin |
| url | https://hdl.handle.net/1721.1/132583.2 |
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