NMR studies have been carried out on subtilisin Carlsberg in order to identify the sharp resonances observed in the proton spectra of the enzyme dissolved in aqueous solution. NMR spectra, obtained with the combination of spin-echo and selective excitation sequences, from both the native and inactivated protein, enabled us to assign sharp signals to subtilisin fragments derived from enzymatic autolysis (monitored by high-performance size-exclusion chromatography), rather than to mobile segments of the intact protein.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
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[NMR paper] Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin
Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR.
Related Articles Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR.
Protein Sci. 2003 Apr;12(4):794-810
Authors: Day RM, Thalhauser CJ, Sudmeier JL, Vincent MP, Torchilin EV, Sanford DG, Bachovchin CW, Bachovchin WW
We have determined by (15)N, (1)H, and (13)C NMR, the chemical behavior of the six histidines in subtilisin BPN' and their PMSF and peptide boronic acid complexes in aqueous solution as a...
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[NMR paper] The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H in
The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.
Related Articles The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.
Proteins. 1996 Jul;25(3):267-85
Authors: Lecomte JT, Kao YH, Cocco MJ
Proton nuclear magnetic resonance spectroscopy was applied to sperm whale apomyoglobin to describe the conformation adopted by the protein under native conditions. The study focused on the A-B-G-H...
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[NMR paper] A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifl
A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones.
Biochemistry. 1996 Dec 10;35(49):15941-8
Authors: Halkides CJ, Wu YQ, Murray CJ
The N delta 1 proton of His 64 forms a hydrogen bond with Asp 32, as part of the catalytic triad in serine proteases of the subtilisin family. His 64 in...
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[MWClarkson blog] How native-like is a cold-denatured structure?
How native-like is a cold-denatured structure?
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngA protein has several different levels of structure. The primary structure is the arrangements of atoms and bonds, and it is formed in the ribosome by the assembly of amino acids as directed by an RNA template. The secondary structure is the local topology, the helices and strands, and this forms mostly because of the release of energy through the formation of hydrogen bonds. The tertiary structure is the actual fold of the protein, the way helices, strands, and loops are...
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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.
Related Articles Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
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
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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08-21-2010 11:12 PM
[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....
H-NMR studies of native and fragmented subtilisin Carlsberg.
Linear Mode
