Related ArticlesContribution of the multi-turn segment in the reversible thermal stability of hyperthermophile rubredoxin: NMR thermal chemical exchange analysis of sequence hybrids.
Biophys Chem. 2005 Jun 1;116(1):57-65
Authors: LeMaster DM, Tang J, Paredes DI, Hernández G
Pyrococcus furiosus (Pf) rubredoxin is the most thermostable protein characterized to date. Reflecting the complications arising from irreversible denaturation of this protein, predictions of which structural regions confer differential thermal stability have utilized kinetic stability measurements, hydrogen exchange protection factors, long range hydrogen bond NMR spin couplings, and molecular dynamics simulations, and have primarily implicated the three-stranded beta-sheet and the adjacent metal binding site. Herein, NMR chemical exchange experiments demonstrate reversible two-state unfolding at the thermal transition temperature (T(m)) for hybrids of Pf and the mesophile Clostridium pasteurianum (Cp) rubredoxins which interchange residues 14-33, the so-called multi-turn segment. This complementary pair of hybrid rubredoxins exhibits largely additive incremental thermal stabilizations vs. the parental proteins. Both stabilization free energy measurements as well as incremental T(m) values indicate that a minimum of 37% of the total differential thermal stability resides in this multi-turn segment. Such a proportionality between DeltaDeltaG and incremental T(m) values is predicted for hybrid pairs exhibiting thermodynamic additivity in which the differential stability is predominantly enthalpic.
Zero-Field NMR Enhancedby Parahydrogen in Reversible Exchange
Zero-Field NMR Enhancedby Parahydrogen in Reversible Exchange
Thomas Theis, Micah P. Ledbetter, Gwendal Kervern, John W. Blanchard, Paul J. Ganssle, Mark C. Butler, Hyun D. Shin, Dmitry Budker and Alexander Pines
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2112405/aop/images/medium/ja-2011-112405_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2112405
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/x6FPOFkzUpk
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[NMR paper] Thermal stability of calmodulin and mutants studied by (1)H-(15)N HSQC NMR measuremen
Thermal stability of calmodulin and mutants studied by (1)H-(15)N HSQC NMR measurements of selectively labeled Ile proteins.
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Biochemistry. 2002 May 28;41(21):6850-9
Authors: Biekofsky RR, Martin SR, McCormick JE, Masino L, Fefeu S, Bayley PM, Feeney J
Calmodulin, the Ca(2+)-dependent activator of many cellular processes, contains two well-defined structural domains, each of which binds two Ca(2+) ions....
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[NMR paper] Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 a
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Biochim Biophys Acta. 2000 Mar 16;1478(1):113-24
Authors: Vu HM, Liu W, Grove A, Geiduschek EP, Kearns DR
A variant of the bacteriophage SPO1-encoded transcription factor 1 (TF1)...
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[NMR paper] Effect of thermal denaturation on water-collagen interactions: NMR relaxation and dif
Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
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Biopolymers. 1999 Dec;50(7):690-6
Authors: Rochdi A, Foucat L, Renou JP
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and...
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[NMR paper] Thermal stability studies of a globular protein in aqueous poly(ethylene glycol) by (
Thermal stability studies of a globular protein in aqueous poly(ethylene glycol) by (1)H NMR.
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Biotechnol Bioeng. 1996 Aug 20;51(4):410-21
Authors: Hancock TJ, Hsu JT
The reversible folding destabilization of hen lysozyme has been confirmed by a melting temperature (T(m)) decrease in aqueous...
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[NMR paper] Membrane protein structure: the contribution and potential of novel solid state NMR a
Membrane protein structure: the contribution and potential of novel solid state NMR approaches.
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Mol Membr Biol. 1995 Jul-Sep;12(3):233-46
Authors: Watts A, Ulrich AS, Middleton DA
Alternative methods for describing molecular detail for large integral membrane proteins are required in the absence of routine crystallographic approaches. Novel solid state NMR methods, devised for the study of large molecular assemblies, are now finding...
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[NMR paper] NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.
NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.
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 NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.
Protein Sci. 1993 May;2(5):851-8
Authors: Kautz RA, Fox RO
Thermally unfolded staphylococcal nuclease has been rapidly...
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Elucidation of the structure and intermolecular interactions of a reversible cyclic-p
Elucidation of the structure and intermolecular interactions of a reversible cyclic-peptide inhibitor of the proteasome by NMR spectroscopy and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Elucidation of the structure and intermolecular interactions of a reversible cyclic-peptide inhibitor of the proteasome by NMR spectroscopy and molecular modeling.
Angew Chem Int Ed Engl. 2010 May 25;49(23):3934-8
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