Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back
Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Laffy, Julie M.J. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Schlagwörter: |
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| Umfang: |
10 |
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| Übergeordnetes Werk: |
Enthalten in: A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital - Ma, Luping ELSEVIER, 2022, an international review journal, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:128 ; year:2017 ; pages:47-56 ; extent:10 |
| Links: |
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| DOI / URN: |
10.1016/j.pbiomolbio.2016.09.002 |
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| 520 | |a Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. | ||
| 520 | |a Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. | ||
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10.1016/j.pbiomolbio.2016.09.002 doi GBV00000000000272A.pica (DE-627)ELV036238848 (ELSEVIER)S0079-6107(16)30047-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Laffy, Julie M.J. verfasserin aut Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Binding promiscuity Elsevier Molecular modelling Elsevier Monte Carlo simulations Elsevier Antibody CDRH3 Elsevier Kidera factors Elsevier Conformational preferences Elsevier ELISA Elsevier Dodev, Tihomir oth Macpherson, Jamie A. oth Townsend, Catherine oth Lu, Hui Chun oth Dunn-Walters, Deborah oth Fraternali, Franca oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:128 year:2017 pages:47-56 extent:10 https://doi.org/10.1016/j.pbiomolbio.2016.09.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 128 2017 47-56 10 045F 570 |
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10.1016/j.pbiomolbio.2016.09.002 doi GBV00000000000272A.pica (DE-627)ELV036238848 (ELSEVIER)S0079-6107(16)30047-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Laffy, Julie M.J. verfasserin aut Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Binding promiscuity Elsevier Molecular modelling Elsevier Monte Carlo simulations Elsevier Antibody CDRH3 Elsevier Kidera factors Elsevier Conformational preferences Elsevier ELISA Elsevier Dodev, Tihomir oth Macpherson, Jamie A. oth Townsend, Catherine oth Lu, Hui Chun oth Dunn-Walters, Deborah oth Fraternali, Franca oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:128 year:2017 pages:47-56 extent:10 https://doi.org/10.1016/j.pbiomolbio.2016.09.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 128 2017 47-56 10 045F 570 |
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10.1016/j.pbiomolbio.2016.09.002 doi GBV00000000000272A.pica (DE-627)ELV036238848 (ELSEVIER)S0079-6107(16)30047-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Laffy, Julie M.J. verfasserin aut Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Binding promiscuity Elsevier Molecular modelling Elsevier Monte Carlo simulations Elsevier Antibody CDRH3 Elsevier Kidera factors Elsevier Conformational preferences Elsevier ELISA Elsevier Dodev, Tihomir oth Macpherson, Jamie A. oth Townsend, Catherine oth Lu, Hui Chun oth Dunn-Walters, Deborah oth Fraternali, Franca oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:128 year:2017 pages:47-56 extent:10 https://doi.org/10.1016/j.pbiomolbio.2016.09.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 128 2017 47-56 10 045F 570 |
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10.1016/j.pbiomolbio.2016.09.002 doi GBV00000000000272A.pica (DE-627)ELV036238848 (ELSEVIER)S0079-6107(16)30047-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Laffy, Julie M.J. verfasserin aut Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Binding promiscuity Elsevier Molecular modelling Elsevier Monte Carlo simulations Elsevier Antibody CDRH3 Elsevier Kidera factors Elsevier Conformational preferences Elsevier ELISA Elsevier Dodev, Tihomir oth Macpherson, Jamie A. oth Townsend, Catherine oth Lu, Hui Chun oth Dunn-Walters, Deborah oth Fraternali, Franca oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:128 year:2017 pages:47-56 extent:10 https://doi.org/10.1016/j.pbiomolbio.2016.09.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 128 2017 47-56 10 045F 570 |
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10.1016/j.pbiomolbio.2016.09.002 doi GBV00000000000272A.pica (DE-627)ELV036238848 (ELSEVIER)S0079-6107(16)30047-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Laffy, Julie M.J. verfasserin aut Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. Binding promiscuity Elsevier Molecular modelling Elsevier Monte Carlo simulations Elsevier Antibody CDRH3 Elsevier Kidera factors Elsevier Conformational preferences Elsevier ELISA Elsevier Dodev, Tihomir oth Macpherson, Jamie A. oth Townsend, Catherine oth Lu, Hui Chun oth Dunn-Walters, Deborah oth Fraternali, Franca oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:128 year:2017 pages:47-56 extent:10 https://doi.org/10.1016/j.pbiomolbio.2016.09.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 128 2017 47-56 10 045F 570 |
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Enthalten in A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital Amsterdam [u.a.] volume:128 year:2017 pages:47-56 extent:10 |
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promiscuous antibodies characterised by their physico-chemical properties: from sequence to structure and back |
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Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back |
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Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. |
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Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. |
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Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity ‘promiscuous’ and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process. |
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