Zobrazeno 1 - 10
of 432
pro vyhledávání: '"Peter E. Wright"'
Autor:
Tom L. Blundell, Peter E. Wright
Publikováno v:
Current Research in Structural Biology, Vol 4, Iss , Pp iv- (2022)
Externí odkaz:
https://doaj.org/article/637acad2caa24c1e82e5c39bf5a5f145
Publikováno v:
Biochemistry. 61:2709-2719
The C-terminal region of the tumor suppressor protein p53 contains three domains, nuclear localization signal (NLS), tetramerization domain (TET), and C-terminal regulatory domain (CTD), which are essential for p53 function. Characterization of the s
Publikováno v:
The Journal of Physical Chemistry B. 126:9539-9548
The earliest events in the folding of a protein are in general poorly understood. We used NMR
Publikováno v:
Nucleic Acids Research. 50:7147-7160
Protein dynamics involving higher-energy sparsely populated conformational substates are frequently critical for protein function. This study describes the dynamics of the homodimer (p50)2 of the p50 Rel homology region (RHR) of the transcription fac
Autor:
H. Jane Dyson, Peter E. Wright
Publikováno v:
Israel Journal of Chemistry.
Autor:
Tom L. Blundell, Peter E. Wright
Publikováno v:
Current research in structural biology. 4
Publikováno v:
FEBS letters.
The cyclic AMP Response Element Binding Protein (CREB) contains a basic leucine zipper motif (bZIP) that forms a coiled coil structure upon dimerization and specific DNA binding. Although this state is well characterized, key features of CREB bZIP bi
Publikováno v:
Biochemistry. 60:2663-2671
Conformational fluctuations from ground-state to sparsely populated but functionally important excited states play a key role in enzyme catalysis. For Escherichia coli dihydrofolate reductase (DHFR), the release of the product tetrahydrofolate (THF)
Publikováno v:
Current Opinion in Chemical Biology. 73:102280
Publikováno v:
The Journal of biological chemistry. 298(8)
Transthyretin (TTR) amyloidosis is associated with tissue deposition of TTR aggregates. TTR aggregation is initiated by dissociation of the native tetramer to form a monomeric intermediate, which locally unfolds and assembles into soluble oligomers a