Related ArticlesElectrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Protein Sci. 1998 Sep;7(9):1930-8
Authors: Kim S, Baum J
alpha-Lactalbumin (alpha-LA) undergoes a pH-dependent unfolding from the native state to a partially unfolded state (the molten globule state). To understand the role of electrostatic interactions in protein denaturation, NMR and CD pH titration experiments are performed on guinea pig alpha-LA. Variation of pH over the range of 7.0 to 2.0 simultaneously leads to the acid denaturation of the protein and the titration of individual ionizable groups. The pH titrations are interpreted in the context of these coupled events, and indicate that acid denaturation in alpha-LA is a cooperative event that is triggered by the protonation of two ionizable residues. Our NMR results suggest that the critical electrostatic interactions that contribute to the denaturation of alpha-LA are concentrated in the calcium binding region of the protein.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
J Biomol NMR. 2011 Sep;51(1-2):5-19
Authors: McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE
Abstract
NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes to...
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Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
J Biomol NMR. 2011 Sep;51(1-2):5-19
Authors: McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE
Abstract
NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes...
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09-30-2011 05:59 AM
[NMR paper] Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequ
Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequent displacement studied by NMR spectroscopy.
Related Articles Adsorption of bovine alpha-lactalbumin on suspended solid nanospheres and its subsequent displacement studied by NMR spectroscopy.
Langmuir. 2004 Jun 22;20(13):5530-8
Authors: Engel MF, Visser AJ, van Mierlo CP
Detailed knowledge of the adsorption-induced conformational changes of proteins is essential to understand the process of protein adsorption. However, not much information about these...
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[NMR paper] Dissecting structural and electrostatic interactions of charged groups in alpha-sarci
Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Related Articles Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Biochemistry. 2003 Nov 18;42(45):13122-33
Authors: García-Mayoral MF, Pérez-Cañadillas JM, Santoro J, Ibarra-Molero B, Sanchez-Ruiz JM, Lacadena J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The cytotoxic ribonuclease...
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[NMR paper] Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR
Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR spectroscopies.
Related Articles Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR spectroscopies.
Biopolymers. 2003 Jun;69(2):176-88
Authors: Yamasaki K, Yamasaki T, Kanaya S, Oobatake M
Acid-induced denaturation of the ribonuclease HI protein from Escherichia coli was analyzed by CD and NMR spectroscopies. The CD measurement revealed that the acid denaturation at 10 degrees C proceeds from the native state (N-state) to a...
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[NMR paper] The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exch
The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
Related Articles The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
J Mol Biol. 2002 Aug 2;321(1):99-110
Authors: Halskau Ø, Frøystein NA, Muga A, Martínez A
The interaction of bovine alpha-lactalbumin (BLA) with negatively charged phospholipid bilayers was studied by NMR monitored 1H exchange to characterize the conformational transition that enables a water-soluble protein to associate with and partially insert...
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[NMR paper] Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Related Articles Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
J Biochem. 1995 Mar;117(3):623-8
Authors: Aramini JM, Hiraoki T, Ke Y, Nitta K, Vogel HJ
The high-affinity calcium-binding sites of bovine and human alpha-lactalbumin as well as equine lysozyme were analyzed by 113Cd NMR spectroscopy. In the case of equine lysozyme, the addition of isotopically enriched 113Cd2+ results in a signal at delta = -75.9 ppm...
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[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Related Articles NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Basic Life Sci. 1990;56:231-53
Authors: Berliner LJ, Kaptein R, Koga K, Musci G