Abstract:
:The recent work is surveyed which leads to the suggestions that the conformation of globular proteins in solution corresponds to a dynamic ensemble of rapidly interconverting spatial structures, that clusters of hydrophobic amino acid side chains have an important role in the architecture of protein molecules, and that mechanistic aspects of protein denaturation can be correlated with internal mobility seen in the native conformation. These conclusions resulted originally from high resolution 1H nuclear magnetic resonance (NMR) studies of aromatic ring mobility, exchange of interior amide protons and thermal denaturation of the basic pancreatic trypsin inhibitor and a group of related proteins. Various new approaches to further characterize proteins in solution have now been taken and preliminary data are presented. These include computer graphics to outline hydrophobic clusters in globular protein structures, high resolution 1H-NMR experiments at variable hydrostatic pressure and 13C-NMR relaxation measurements. At the present early stage of these new investigations it appears that the hydrophobic cluster model for globular proteins is compatible with the data obtained.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Wüthrich K,Wagner G,Richarz R,Braun Wdoi
10.1016/S0006-3495(80)84989-7subject
Has Abstractpub_date
1980-10-01 00:00:00pages
549-60issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(80)84989-7journal_volume
32pub_type
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