Related ArticlesNMR, alcohols, protein solvation and protein denaturation.
EXS. 1994;71:261-8
Authors: Wüthrich K
The amino acid side chains of Ser, Thr and Tyr contain the hydroxyl functional group that is characteristic of alcohols, and a variety of different alcohols are used either as structure-inducing or denaturing co-solvents in physical-chemical studies of proteins. This article surveys selected aspects of the influence of protein-intrinsic and -extrinsic hydroxyl groups on studies of the solvation of peptides and proteins by nuclear magnetic resonance (NMR) spectroscopy.
[NMR paper] A compact monomeric intermediate identified by NMR in the denaturation of dimeric tri
A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.
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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] Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of
Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
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] NMR, alcohols, protein solvation and protein denaturation.
NMR, alcohols, protein solvation and protein denaturation.
Related Articles NMR, alcohols, protein solvation and protein denaturation.
EXS. 1994;71:261-8
Authors: Wüthrich K
The amino acid side chains of Ser, Thr and Tyr contain the hydroxyl functional group that is characteristic of alcohols, and a variety of different alcohols are used either as structure-inducing or denaturing co-solvents in physical-chemical studies of proteins. This article surveys selected aspects of the influence of protein-intrinsic and -extrinsic hydroxyl groups on...
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[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
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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] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold 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....
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
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
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] NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and co
NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
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Q Rev Biophys. 1999 Feb;32(1):57-98
Authors: Härd T
NMR, alcohols, protein solvation and protein denaturation.
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