- Abstract:
-
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 pr...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/jp952747v
-
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- Journal:
- JOURNAL OF PHYSICAL CHEMISTRY
- Volume:
- 100
- Issue:
- 7
- Pages:
- 2661-2666
- Publication date:
- 1996-02-15
- DOI:
- EISSN:
-
1541-5740
- ISSN:
-
0022-3654
- URN:
-
uuid:ba0adf3c-1513-4556-b1cb-9b24edc677ad
- Source identifiers:
-
45092
- Local pid:
- pubs:45092
- Copyright date:
- 1996
Journal article
Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements
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