Processing helix–coil transition data: Account of chain length and solvent effects
Numerous nanobiotechnologies include manipulations of short polypeptide chains. The conformational properties of these polypeptides are studied in vitro by circular dichroism and time-resolved infrared spectroscopy. To find out the interaction parameters, the measured temperature dependence of norma...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-10-01
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| Series: | Frontiers in Nanotechnology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fnano.2022.982644/full |
| _version_ | 1811239661245300736 |
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| author | Knarik Yeritsyan Matjaz Valant Artem Badasyan |
| author_facet | Knarik Yeritsyan Matjaz Valant Artem Badasyan |
| author_sort | Knarik Yeritsyan |
| collection | DOAJ |
| description | Numerous nanobiotechnologies include manipulations of short polypeptide chains. The conformational properties of these polypeptides are studied in vitro by circular dichroism and time-resolved infrared spectroscopy. To find out the interaction parameters, the measured temperature dependence of normalized helicity degree needs to be further processed by fitting to a model. Using recent advances in the Hamiltonian formulation of the classical Zimm and Bragg model, we explicitly include chain length and solvent effects in the theoretical description. The expression for the helicity degree we suggest successfully fits the experimental data and provides hydrogen bonding energies and nucleation parameter values within the standards in the field. |
| first_indexed | 2024-04-12T13:05:03Z |
| format | Article |
| id | doaj.art-b9ebb44bdf6b43ffbb0a286abb804504 |
| institution | Directory Open Access Journal |
| issn | 2673-3013 |
| language | English |
| last_indexed | 2024-04-12T13:05:03Z |
| publishDate | 2022-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Nanotechnology |
| spelling | doaj.art-b9ebb44bdf6b43ffbb0a286abb8045042022-12-22T03:32:04ZengFrontiers Media S.A.Frontiers in Nanotechnology2673-30132022-10-01410.3389/fnano.2022.982644982644Processing helix–coil transition data: Account of chain length and solvent effectsKnarik YeritsyanMatjaz ValantArtem BadasyanNumerous nanobiotechnologies include manipulations of short polypeptide chains. The conformational properties of these polypeptides are studied in vitro by circular dichroism and time-resolved infrared spectroscopy. To find out the interaction parameters, the measured temperature dependence of normalized helicity degree needs to be further processed by fitting to a model. Using recent advances in the Hamiltonian formulation of the classical Zimm and Bragg model, we explicitly include chain length and solvent effects in the theoretical description. The expression for the helicity degree we suggest successfully fits the experimental data and provides hydrogen bonding energies and nucleation parameter values within the standards in the field.https://www.frontiersin.org/articles/10.3389/fnano.2022.982644/fullshort polypeptide chainshelix-coildegree of helicitywater modelZimm and Bragg model |
| spellingShingle | Knarik Yeritsyan Matjaz Valant Artem Badasyan Processing helix–coil transition data: Account of chain length and solvent effects Frontiers in Nanotechnology short polypeptide chains helix-coil degree of helicity water model Zimm and Bragg model |
| title | Processing helix–coil transition data: Account of chain length and solvent effects |
| title_full | Processing helix–coil transition data: Account of chain length and solvent effects |
| title_fullStr | Processing helix–coil transition data: Account of chain length and solvent effects |
| title_full_unstemmed | Processing helix–coil transition data: Account of chain length and solvent effects |
| title_short | Processing helix–coil transition data: Account of chain length and solvent effects |
| title_sort | processing helix coil transition data account of chain length and solvent effects |
| topic | short polypeptide chains helix-coil degree of helicity water model Zimm and Bragg model |
| url | https://www.frontiersin.org/articles/10.3389/fnano.2022.982644/full |
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