Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins
The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1973 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Protein Structure - Amsterdam : Elsevier, 328(1973), 1, Seite 10-19 |
| Übergeordnetes Werk: |
volume:328 ; year:1973 ; number:1 ; pages:10-19 |
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| 245 | 1 | 0 | |a Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins |
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| 520 | |a The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. | ||
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(DE-627)NLEJ186075529 (DE-599)GBVNLZ186075529 DE-627 ger DE-627 rakwb eng Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bradbury, J.H. oth Norton, R.S. oth in BBA - Protein Structure Amsterdam : Elsevier 328(1973), 1, Seite 10-19 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:328 year:1973 number:1 pages:10-19 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90324-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 328 1973 1 10-19 |
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(DE-627)NLEJ186075529 (DE-599)GBVNLZ186075529 DE-627 ger DE-627 rakwb eng Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bradbury, J.H. oth Norton, R.S. oth in BBA - Protein Structure Amsterdam : Elsevier 328(1973), 1, Seite 10-19 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:328 year:1973 number:1 pages:10-19 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90324-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 328 1973 1 10-19 |
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(DE-627)NLEJ186075529 (DE-599)GBVNLZ186075529 DE-627 ger DE-627 rakwb eng Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bradbury, J.H. oth Norton, R.S. oth in BBA - Protein Structure Amsterdam : Elsevier 328(1973), 1, Seite 10-19 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:328 year:1973 number:1 pages:10-19 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90324-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 328 1973 1 10-19 |
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(DE-627)NLEJ186075529 (DE-599)GBVNLZ186075529 DE-627 ger DE-627 rakwb eng Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bradbury, J.H. oth Norton, R.S. oth in BBA - Protein Structure Amsterdam : Elsevier 328(1973), 1, Seite 10-19 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:328 year:1973 number:1 pages:10-19 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90324-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 328 1973 1 10-19 |
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(DE-627)NLEJ186075529 (DE-599)GBVNLZ186075529 DE-627 ger DE-627 rakwb eng Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bradbury, J.H. oth Norton, R.S. oth in BBA - Protein Structure Amsterdam : Elsevier 328(1973), 1, Seite 10-19 (DE-627)NLEJ176858709 (DE-600)2209544-5 0005-2795 nnns volume:328 year:1973 number:1 pages:10-19 http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90324-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 328 1973 1 10-19 |
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carbon-13 nmr spectra of tryptophan, tryptophan peptides and of native and denatured proteins |
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Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins |
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The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. |
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The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. |
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The assignment of the carbon-13 magnetic resonance spectrum of l-tryptophan in aqueous solution and in trifluoroacetic acid is made by comparison with the spectra of indoles, by double resonance and by deuteration experiments. On the basis of work on small peptides, it is possible to assign all the downfield resonances in denatured proteins to single types of carbon atoms, with the exception of the carbonyl carbons and the histidine Cγ resonance. In the upfield region there are only about eleven resonances which correspond to single types of carbon atoms from eight different amino acid residues. The spectra of a particular protein denatured by heat, 6 M guanidine . HCl or formic acid are all similar. The spectrum of a native protein is much broader than that of the denatured protein due to small differences in chemical shift which result from environmental changes of some carbon atoms, and line broadening due to decreased mobility of carbon atoms. |
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