Related ArticlesNMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been investigated in H2O and TFE/H2O solution by CD and NMR to gain insight into the possible role that native beta-hairpin secondary structure elements may have in early protein folding steps. The fragment also has been studied under denaturing conditions (6 M urea), and the resulting NMR chemical shifts were used as a reference for the disordered state. On the basis of CD and NMR data, it is concluded that in aqueous solution the fragment is basically flexible, with two local low populated chain bends involving residues 8-9 and 14-15, respectively, in close agreement with secondary structure predictions, a structure that is different from the final folded state of that segment of the protein. The changes in the CD spectrum, the presence of several medium-range NOEs plus two long-range NOEs, and the sign of the H alpha conformational shifts reveal that the addition of TFE facilitates the formation of a set of transient beta-hairpins involving essentially the same residues that form the native beta-hairpin found in the final three-dimensional structure of the B1 domain. The stabilization of native-like structures by TFE is known to occur for helices, but, to our knowledge, this is the first time the stabilization of a native-like beta-hairpin structure by TFE is reported. Since long-range tertiary interactions are absent in the isolated fragment, our results support the idea that, in addition to helices, beta-hairpins may play an active role in directing the protein folding process.
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray cr
NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.
Related Articles NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.
Biopolymers. 2002 Feb;63(2):111-21
Authors: Kowalski JA, Liu K, Kelly JW
The NMR solution structure of the isolated Apo Pin1 WW domain (6-39) reveals that it adopts a twisted three-stranded antiparallel beta-sheet conformation, very similar to the structure exhibited by the crystal of this domain in the...
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NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-ŕ-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
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[NMR paper] Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and C
Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues.
Related Articles Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues.
Protein Eng. 1996 Jul;9(7):559-65
Authors: Searle MS, Zerella R, Williams DH, Packman LC
The conformational properties of protein fragments have been widely studied as models of the earliest initiation events in protein folding. While...
NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev
Linear Mode
