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...

Full description

Bibliographic Details
Main Authors: Fiebig, K, Schwalbe, H, Buck, M, Smith, L, Dobson, C
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