Related ArticlesA compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.
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 absence of denaturant, the hydrodynamic radius of 29.6(+/-0.25) A and the substantial chemical shift dispersion evident in the NMR spectrum are consistent with the highly structured dimeric native state of the protein. On the addition of 2. 2 M guanidine hydrochloride the effective hydrodynamic radius increases to 51.4(+/-0.43) A, consistent with that anticipated for the polypeptide chain in a highly unstructured random coil state. In 1.1 M guanidine hydrochloride, however, the effective hydrodynamic radius is 24.0(+/-0.25) A, a value substantially decreased relative to that of the native dimeric state but very close to that anticipated for a monomeric species with native-like compaction (23. 5 A). The lack of chemical shift dispersion indicates, however, that few tertiary interactions persist within this species. Far UV CD and intrinsic fluorescence measurements show that this compact intermediate retains significant secondary structure and that on average the fluorophores are partially excluded from solvent. Such a species could be important in the formation of dimeric TIM from its unfolded state.
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[NMR paper] The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate s
The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Related Articles The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30
Authors: Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kühne R, Bermel W, Bacher A, Richter G, Oschkinat H
Recent developments in...
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11-19-2010 08:44 PM
[NMR paper] Design and NMR analyses of compact, independently folded BBA motifs.
Design and NMR analyses of compact, independently folded BBA motifs.
Related Articles Design and NMR analyses of compact, independently folded BBA motifs.
Fold Des. 1998;3(2):95-103
Authors: Struthers M, Ottesen JJ, Imperiali B
BACKGROUND: Small folded polypeptide motifs represented highly simplified systems for theoretical and experimental studies on protein structure and folding. We have recently reported the design and characterization of a metal-ion-independent 23-residue peptide with a beta beta alpha structure (BBA1), based on the zinc...
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[NMR paper] Structure of a compact peptide from staphylococcal nuclease determined by circular di
Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy.
Related Articles Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy.
Biochemistry. 1995 May 2;34(17):5795-800
Authors: Maciejewski MW, Zehfus MH
Compact regions in proteins are thought to correspond to domains. If this is true, the structure of a compact region excised from a protein should closely resemble the structure in the intact protein. To test this theory, a...
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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] 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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[Stan NMR blog] Compact permanent magnets for time-domain NMR
Compact permanent magnets for time-domain NMR
Compact MR-quality permanent magnets available off the shelf up to 0.5 T
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[NMR paper] NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synth
NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling.
Eur J Biochem. 1999 Apr;261(1):57-65
Authors: Richter G, Kelly M, Krieger C, Yu Y, Bermel W, Karlsson G, Bacher A, Oschkinat H
...
A compact monomeric intermediate identified by NMR in the denaturation of dimeric tri
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