Structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures
Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differen...
Ausführliche Beschreibung
Autor*in: |
Zhang, X Y [verfasserIn] |
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Artikel |
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Sprache: |
Englisch |
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2015 |
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Schlagwörter: |
Superoxide Dismutase - chemistry |
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Übergeordnetes Werk: |
Enthalten in: Nanotechnology - Bristol : IOP Publishing Ltd., 1990, 26(2015), 12 |
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Übergeordnetes Werk: |
volume:26 ; year:2015 ; number:12 |
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520 | |a Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the α-domain and β-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single α-domain protein hemoglobin (Hgb) and a β-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the α-domain is more conductive. To confirm our finding, molecular orbitals of both the β-domain in SOD and α-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the α-domain are both more efficient, indicating that it is easier for electrons to transport through the α-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of α- and β-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the α-domain and β-domain. This research should be very important to application prospects in molecular electronics. | ||
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PQ20160617 (DE-627)OLC1958743631 (DE-599)GBVOLC1958743631 (PRQ)pubmed_primary_257365490 (KEY)0198956120150000026001200000structuredependentelectricalconductivityofproteini DE-627 ger DE-627 rakwb eng 530 DNB Zhang, X Y verfasserin aut Structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the α-domain and β-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single α-domain protein hemoglobin (Hgb) and a β-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the α-domain is more conductive. To confirm our finding, molecular orbitals of both the β-domain in SOD and α-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the α-domain are both more efficient, indicating that it is easier for electrons to transport through the α-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of α- and β-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the α-domain and β-domain. This research should be very important to application prospects in molecular electronics. Superoxide Dismutase - chemistry Microscopy, Scanning Tunneling - methods Hemoglobins - chemistry Shao, Jian oth Jiang, S X oth Wang, Biao oth Zheng, Yue oth Enthalten in Nanotechnology Bristol : IOP Publishing Ltd., 1990 26(2015), 12 (DE-627)130923141 (DE-600)1054118-4 (DE-576)025181165 0957-4484 nnns volume:26 year:2015 number:12 http://www.ncbi.nlm.nih.gov/pubmed/25736549 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_170 GBV_ILN_2005 GBV_ILN_4126 AR 26 2015 12 |
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structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures |
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Structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures |
abstract |
Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the α-domain and β-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single α-domain protein hemoglobin (Hgb) and a β-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the α-domain is more conductive. To confirm our finding, molecular orbitals of both the β-domain in SOD and α-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the α-domain are both more efficient, indicating that it is easier for electrons to transport through the α-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of α- and β-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the α-domain and β-domain. This research should be very important to application prospects in molecular electronics. |
abstractGer |
Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the α-domain and β-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single α-domain protein hemoglobin (Hgb) and a β-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the α-domain is more conductive. To confirm our finding, molecular orbitals of both the β-domain in SOD and α-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the α-domain are both more efficient, indicating that it is easier for electrons to transport through the α-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of α- and β-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the α-domain and β-domain. This research should be very important to application prospects in molecular electronics. |
abstract_unstemmed |
Electron transports in the α-domain and β-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the α-domain and β-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single α-domain protein hemoglobin (Hgb) and a β-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the α-domain is more conductive. To confirm our finding, molecular orbitals of both the β-domain in SOD and α-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the α-domain are both more efficient, indicating that it is easier for electrons to transport through the α-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of α- and β-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the α-domain and β-domain. This research should be very important to application prospects in molecular electronics. |
collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_170 GBV_ILN_2005 GBV_ILN_4126 |
container_issue |
12 |
title_short |
Structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures |
url |
http://www.ncbi.nlm.nih.gov/pubmed/25736549 |
remote_bool |
false |
author2 |
Shao, Jian Jiang, S X Wang, Biao Zheng, Yue |
author2Str |
Shao, Jian Jiang, S X Wang, Biao Zheng, Yue |
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up_date |
2024-07-03T14:23:54.328Z |
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