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Molecular hinges in protein folding : the urea-denatured state of apomyoglobin

Title data

Schwarzinger, Stephan ; Wright, Peter E. ; Dyson, H. Jane:
Molecular hinges in protein folding : the urea-denatured state of apomyoglobin.
In: Biochemistry. Vol. 41 (2002) Issue 42 . - pp. 12681-12686.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi020381o

Abstract in another language

Unfolded apomyoglobin in 8 M urea at pH 2.3 displays distinct regions with different backbone mobility, as monitored by NMR relaxation. These variations in backbone mobility can be correlated with intrinsic properties of the amino acids in the sequence. Clusters of small amino acids such as glycine and alanine show increased backbone mobility compared to the average. In contrast, local hydrophobic interactions that persist in urea denaturant cause some restriction of backbone motions on a picosecond to nanosecond time scale. The model derived from the behavior of apoMb in urea depends only on the most fundamental properties of the local amino acid sequence, and thus provides a feasible paradigm for the initiation of folding.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 25 Jan 2019 10:08
Last Modified: 16 May 2019 05:37
URI: https://eref.uni-bayreuth.de/id/eprint/47039