Related ArticlesCold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range. Assignments of some of the 1H NMR signals of SSI in the cold-denatured and heat-denatured states were performed by a combined use of selective deuteration and site-directed mutagenesis. Throughout the pH range from 2.1 to 3.1, both transitions were cooperative and basically only three distinct spectra corresponding to structures in the cold-denatured, native, and heat-denatured states were detected. In the cold-denatured state, the side-chain signals of Met73, His106, at least one Val, and two Leu were observed at distinctly shifted positions from those for a random-coiled structure, suggesting the formation of a tertiary structure, while those of Met70, His43, and Ala2 were observed at positions for a random-coiled structure. This tertiary structure in the cold-denatured state is entirely different from that in the native state, as some amino acid residues exposed to the solvent in the native state (e.g., Met73, His106) are buried while those sequestered in the native state (e.g., His43) are exposed. In the heat-denatured state, however, most 1H NMR signals were observed at random-coiled positions, indicating that there is much less tertiary structure in the heat-denatured state than in the cold-denatured state. At pH values below 2.09, a structural transition was observed from the cold-denatured state to the heat-denatured state without passing through the native state.(ABSTRACT TRUNCATED AT 250 WORDS)
[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.
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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] A compact monomeric intermediate identified by NMR in the denaturation of dimeric tri
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J Mol Biol. 2000 Jun 30;300(1):11-6
Authors: Morgan CJ, Wilkins DK, Smith LJ, Kawata Y, Dobson CM
The denaturation of triose phosphate isomerase (TIM) from Saccharomyces cerevisiae by guanidine hydrochlorids at pH 7.2 has been monitored by NMR spectroscopy in conjunction with optical spectroscopy. In the...
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[NMR paper] Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined b
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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...
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[NMR paper] Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of
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J Mol Biol. 1996 Jun 21;259(4):805-18
Authors: Wong KB, Freund SM, Fersht AR
Detection of residual structure in denatured proteins is of interest because fleetingly structured regions may be initiation points of the...
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[NMR paper] Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin
Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
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J Biomol NMR. 1991 May;1(1):49-64
Authors: Uchida K, Miyake Y, Kainosho M
Four enhanced carbonyl carbon resonances were observed when Streptomyces subtilisin inhibitor (SSI) was labeled by...
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[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
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Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
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J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
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J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...