Abstract:
:The conformational analysis of non-native states of proteins remains one of the most difficult problems in structural biology, because such states are represented by a superimposition of several states that are rapidly interconverting. Hence, model building of the conformational ensemble remains challenging, although many different biophysical observables can be determined in non-native states of proteins. Here, we present a comprehensive analysis of non-native states of wild-type and mutant forms of the model protein lysozyme by nuclear magnetic resonance spectroscopy. Relaxation rates, chemical shifts, backbone and side chain coupling constants, residual dipolar couplings, diffusion rate constants, and small-angle scattering data merged with computational approaches, such as flexible meccano and ASTEROIDS, allow the description of the non-native state of hen egg white lysozyme in unprecedented detail.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Sziegat F,Silvers R,Hähnke M,Jensen MR,Blackledge M,Wirmer-Bartoschek J,Schwalbe Hdoi
10.1021/bi300222fsubject
Has Abstractpub_date
2012-04-24 00:00:00pages
3361-72issue
16eissn
0006-2960issn
1520-4995journal_volume
51pub_type
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