Related ArticlesA pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.
Biochemistry. 1997 Mar 18;36(11):3383-8
Authors: Ilyina E, Roongta V, Pan H, Woodward C, Mayo KH
Previous studies have produced conflicting interpretations regarding the aggregation state of BPTI in solution. Here, pulsed-field gradient NMR self-association measurements have been performed with BPTI under a variety of temperature, pH, salt, urea conditions, and protein concentrations. Relative to the standard proteins, lysozyme, ribonuclease, and ubiquitin, diffusion constants indicate that BPTI dimerizes at concentrations above about 3 mg/mL and below 280 K. At higher temperatures, a marked self-association is observed above 10 mg/mL. The apparent lack of significant effects from variations in pH and NaCl concentration suggests minimal contribution to the aggregation process from charge-charge interactions. In contrast, in nondenaturing concentrations of urea (2 M), BPTI behaves as a monomer, suggesting that hydrophobic and polar residues modulate BPTI association. The BPTI surface shows that while one side is highly charged, the opposite side, composed mostly of hydrophobic and some hydrophilic residues, is feasible as an interface for BPTI self-association.
[NMR paper] NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal u
NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability.
Related Articles NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability.
J Mol Biol. 2002 Aug 23;321(4):647-58
Authors: Cierpicki T, Otlewski J
Here we determined NMR solution structures of two mutants of bovine pancreatic trypsin inhibitor (BPTI) to reveal structural reasons of their decreased...
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[NMR paper] Characterization of the interaction between bovine pancreatic trypsin inhibitor and t
Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR.
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Biophys Chem. 1998 Apr 20;71(2-3):221-34
Authors: Jolivalt C, Böckmann A, Riès-Kautt M, Ducruix A, Guittet E
The interaction between Bovine Pancreatic Trypsin Inhibitor and thiocyanate was studied using NMR spectroscopy following several experimental approaches. The chemical shift variations of the BPTI protons in the...
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[NMR paper] Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partiall
Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor.
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 Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor.
Protein Sci. 1997...
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[NMR paper] A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
Biophys Chem. 1997 Apr 22;65(2-3):179-87
Authors: Price WS, Nara M, Arata Y
Pulsed field gradient NMR is a convenient alternative to traditional methods for measuring diffusion of biological macromolecules. In the present study, pulsed field gradient NMR was...
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[NMR paper] A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
Biophys Chem. 1997 Apr 22;65(2-3):179-87
Authors: Price WS, Nara M, Arata Y
Pulsed field gradient NMR is a convenient alternative to traditional methods for measuring diffusion of biological macromolecules. In the present study, pulsed field gradient NMR was...
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08-22-2010 03:03 PM
[NMR paper] A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-associa
A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.
Biochemistry. 1997 Mar 18;36(11):3383-8
Authors: Ilyina E, Roongta V, Pan H, Woodward C, Mayo KH
Previous studies have produced conflicting interpretations regarding the aggregation state of BPTI in solution. Here, pulsed-field gradient NMR self-association...
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08-22-2010 03:03 PM
[NMR paper] Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: appl
Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2.
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J Biomol NMR. 1995 Nov;6(3):321-8
Authors: Dingley AJ, Mackay JP, Chapman BE, Morris MB, Kuchel PW, Hambly BD, King GF
At the millimolar concentrations required for structural studies, NMR spectra of the calcium-binding protein myosin light chain 2 (MLC2) showed resonance line widths indicative...
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[NMR paper] Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison
Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations.
J Mol Biol. 1995 Feb 17;246(2):356-65
Authors: Smith PE, van Schaik RC, Szyperski T, Wüthrich K, van Gunsteren WF
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