Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements
A strategy is proposed to describe the backbone conformations sampled in denatured states of proteins. Main chain dihedral angle distributions are extracted from the protein data base and used to predict NMR parameters such as coupling constants and NOE intensities. A simple model in which each resi...
Main Authors: | , , , , |
---|---|
Format: | Journal article |
Published: |
1996
|
_version_ | 1797091157570748416 |
---|---|
author | Fiebig, K Schwalbe, H Buck, M Smith, L Dobson, C |
author_facet | Fiebig, K Schwalbe, H Buck, M Smith, L Dobson, C |
author_sort | Fiebig, K |
collection | OXFORD |
description | A strategy is proposed to describe the backbone conformations sampled in denatured states of proteins. Main chain dihedral angle distributions are extracted from the protein data base and used to predict NMR parameters such as coupling constants and NOE intensities. A simple model in which each residue samples its φ,ψ distribution noncooperatively has been found to reproduce many of the features of experimental NMR data for hen egg-white lysozyme denatured in 8 M urea at low pH. This model provides a framework which allows identification of residual structure inherent in experimental data of nonnative states of proteins. The effects of introducing local conformational cooperativity on NMR parameters are discussed and analyzed in light of the experimental data for lysozyme. © 1996 American Chemical Society. |
first_indexed | 2024-03-07T03:29:00Z |
format | Journal article |
id | oxford-uuid:ba0adf3c-1513-4556-b1cb-9b24edc677ad |
institution | University of Oxford |
last_indexed | 2024-03-07T03:29:00Z |
publishDate | 1996 |
record_format | dspace |
spelling | oxford-uuid:ba0adf3c-1513-4556-b1cb-9b24edc677ad2022-03-27T05:07:13ZToward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurementsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ba0adf3c-1513-4556-b1cb-9b24edc677adSymplectic Elements at Oxford1996Fiebig, KSchwalbe, HBuck, MSmith, LDobson, CA strategy is proposed to describe the backbone conformations sampled in denatured states of proteins. Main chain dihedral angle distributions are extracted from the protein data base and used to predict NMR parameters such as coupling constants and NOE intensities. A simple model in which each residue samples its φ,ψ distribution noncooperatively has been found to reproduce many of the features of experimental NMR data for hen egg-white lysozyme denatured in 8 M urea at low pH. This model provides a framework which allows identification of residual structure inherent in experimental data of nonnative states of proteins. The effects of introducing local conformational cooperativity on NMR parameters are discussed and analyzed in light of the experimental data for lysozyme. © 1996 American Chemical Society. |
spellingShingle | Fiebig, K Schwalbe, H Buck, M Smith, L Dobson, C Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title | Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title_full | Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title_fullStr | Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title_full_unstemmed | Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title_short | Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements |
title_sort | toward a description of the conformations of denatured states of proteins comparison of a random coil model with nmr measurements |
work_keys_str_mv | AT fiebigk towardadescriptionoftheconformationsofdenaturedstatesofproteinscomparisonofarandomcoilmodelwithnmrmeasurements AT schwalbeh towardadescriptionoftheconformationsofdenaturedstatesofproteinscomparisonofarandomcoilmodelwithnmrmeasurements AT buckm towardadescriptionoftheconformationsofdenaturedstatesofproteinscomparisonofarandomcoilmodelwithnmrmeasurements AT smithl towardadescriptionoftheconformationsofdenaturedstatesofproteinscomparisonofarandomcoilmodelwithnmrmeasurements AT dobsonc towardadescriptionoftheconformationsofdenaturedstatesofproteinscomparisonofarandomcoilmodelwithnmrmeasurements |