Related ArticlesInsights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
J Pept Res. 2003 Apr;61(4):177-88
Authors: Santiveri CM, Rico M, Jiménez MA, Pastor MT, Pérez-Payá E
In a previous study we designed a 20-residue peptide able to adopt a significant population of a three-stranded antiparallel beta-sheet in aqueous solution (de Alba et al. [1999]Protein Sci.8, 854-865). In order to better understand the factors contributing to beta-sheet folding and stability we designed and prepared nine variants of the parent peptide by substituting residues at selected positions in its strands. The ability of these peptides to form the target motif was assessed on the basis of NMR parameters, in particular NOE data and 13Calpha conformational shifts. The populations of the target beta-sheet motif were lower in the variants than in the parent peptide. Comparative analysis of the conformational behavior of the peptides showed that, as expected, strand residues with low intrinsic beta-sheet propensities greatly disfavor beta-sheet folding and that, as already found in other beta-sheet models, specific cross-strand side chain-side chain interactions contribute to beta-sheet stability. More interestingly, the performed analysis indicated that the destabilization effect of the unfavorable strand residues depends on their location at inner or edge strands, being larger at the latter. Moreover, in all the cases examined, favorable cross-strand side chain-side chain interactions were not strong enough to counterbalance the disfavoring effect of a poor beta-sheet-forming residue, such as Gly.
[NMR paper] QSAR-by-NMR: quantitative insights into structural determinants for binding affinity
QSAR-by-NMR: quantitative insights into structural determinants for binding affinity by analysis of 1H/15N chemical shift differences in MMP-3 ligands.
Related Articles QSAR-by-NMR: quantitative insights into structural determinants for binding affinity by analysis of 1H/15N chemical shift differences in MMP-3 ligands.
Bioorg Med Chem Lett. 2005 Apr 1;15(7):1779-83
Authors: Matter H, Schudok M, Elshorst B, Jacobs DM, Saxena K, Kogler H
A novel strategy is applied to obtain quantitative insights on factors influencing biological affinity in...
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[NMR paper] The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty
The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Related Articles The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Protein Sci. 2004 May;13(5):1227-37
Authors: Ogbay B, Dekoster GT, Cistola DP
Intestinal fatty acid-binding protein (I-FABP) has a clam-shaped structure that may serve as a scaffold for the design of artificial enzymes and drug carriers. In an attempt to optimize the scaffold for increased access to the...
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[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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[NMR paper] Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Related Articles Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Fold Des. 1998;3(5):313-20
Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS
BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals...
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[NMR paper] 2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to therm
2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to thermostability.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to thermostability.
Protein Sci. 1996 May;5(5):883-94
Authors: Richie KA, Teng Q, Elkin CJ, Kurtz DM
...
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[NMR paper] NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment compleme
NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Related Articles NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Proteins. 1995 May;22(1):41-4
Authors: Tasayco ML, Chao K
The study of complementary protein fragments is thought to be generally useful to identify early folding intermediates. A prerequisite for these studies is the reconstitution of the native-like structure by fragment complementation. Structural analysis of the complementation of the...
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[NMR paper] 1H NMR identification of a beta-sheet structure and description of folding topology i
1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Related Articles 1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Biochemistry. 1991 Apr 23;30(16):3850-6
Authors: Pochapsky TC, Ye XM
Putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a cluster, is the physiological reductant of P-450cam, which in turn catalyzes the monohydroxylation of camphor by molecular oxygen. No crystal structure has...