(Q39948007)

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Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Strategies for assignments

scientific article published on August 25, 1975

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scholarly article

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Europe PubMed Central

15 September 2017

Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Strategies for assignments (English)

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10.1016/S0021-9258(19)41077-6

https://api.crossref.org/works/10.1016/S0021-9258(19)41077-6

21 December 2022

1 reference

10.1016/S0021-9258(19)41077-6

https://api.crossref.org/works/10.1016/S0021-9258(19)41077-6

21 December 2022

1 reference

10.1016/S0021-9258(19)41077-6

https://api.crossref.org/works/10.1016/S0021-9258(19)41077-6

21 December 2022

author name string

E. Oldfield

1

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A169240

21 December 2022

R. S. Norton

2

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A169240

21 December 2022

A. Allerhand

3

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21 December 2022

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publication date

1 August 1975

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Europe PubMed Central

15 September 2017

25 August 1975

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=169240

21 December 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/250/16/6381

online access status

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Europe PubMed Central

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21 December 2022

https://api.elsevier.com/content/article/PII:S0021925819410776?httpAccept=text/xml

1 reference

10.1016/S0021-9258(19)41077-6

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21 December 2022

https://api.elsevier.com/content/article/PII:S0021925819410776?httpAccept=text/plain

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10.1016/S0021-9258(19)41077-6

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21 December 2022

Journal of Biological Chemistry

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Europe PubMed Central

15 September 2017

250

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Europe PubMed Central

15 September 2017

6381-6402

1 reference

Europe PubMed Central

15 September 2017

16

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Europe PubMed Central

15 September 2017

Natural-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Numerous single-carbon resonances of hen egg-white lysozyme

1

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Cytochrome c: observation of numerous single-carbon sites of the reduced and oxidized species by means of natural-abundance 13C nuclear magnetic resonance spectroscopy

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Carbon-13 Fourier transform NMR studies in 20 mm sample tubes: observation of individual carbon sites in proteins

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Magnetic resonance studies of macromolecules. I. Aromatic-methyl interactions and helical structure effects in lysozyme

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Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonance

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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. II. Spectral assignments and inhibitor binding in hen egg-white lysozyme

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Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme

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Perturbation of the PMR spectrum of lysozyme by Co+2

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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. I. Histidine residues

13

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Proton magnetic resonance spectroscopy of histidine residues in proteins

14

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Spin-label-induced nuclear relaxation. Distances between bound saccharides, histidine-15, and tryptophan-123 on lysozyme in solution

15

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Assignment of tryptophan indole NH proton resonances of lysozyme

16

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Proton magnetic resonance study of the indole NH resonances of lysozyme. Assignment, deuterium exchange kinetics, and inhibitor binding

17

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21 December 2022

The determination of the structure of proteins in solution: lysozyme

18

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High-resolution proton nuclear magnetic resonance spectroscopy of cytochrome

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Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy

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Proton magnetic resonance studies of horse cytochrome c.

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21 December 2022

Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome c

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Proton magnetic resonance evidence for methionine-iron coordination in mammalian-type ferrocytochrome c

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Pulsed NMR study of the structure of cytochrome c

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NMR double resonance study of azidoferricytochrome c

31

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High-resolution proton magnetic resonance spectra of sperm whale cyanometmyoglobin

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Nuclear magnetic resonance study of cyanoferrimyoglobin; Identification of pseudocontact shifts

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Nuclear magnetic resonances of reconstituted myoglobins

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Proton nuclear magnetic resonance studies of myoglobin in H2O

35

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Proton magnetic resonance study of the histidine residues of horse myoglobin

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Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuteration

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Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins

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Nuclear magnetic resonance determination of ligand-induced conformational changes in myoglobin

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21 December 2022

Natural abundance fourier transform of 13C nuclear magnetic resonance spectra of lysozyme

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Carbon-13 nuclear-magnetic-resonance studies on selected amino acids, peptides, and proteins

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Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins

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Natural abundance 13C spectra of proteins: Carboxy-myoglobin and hemoglobin

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Thermodynamics of the redox reaction of cytochromes c of five different species

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The position of the active tryptophan residue in lysozyme

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Nuclear magnetic resonance spectroscopy. Carbon-13 chemical shifts of small peptides as a function of pH

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The identification of histidine-15 as part of an esteratic site of hen's egg white lysozyme

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A new approach to the determination of pKa's of histidine residues in proteins

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13C nuclear magnetic resonance spectra of coproporphyrins

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Recent developments in the investigation of the paramagnetic centers in low-spin ferric hemoproteins: carbon-13 hyperfine shifts in iron porphyrin complexes

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Denaturation of proteins. V. N.M.R. study of the arginine residues of lysozyme

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Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopy

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Assignments in the carbon-13 nuclear magnetic resonance spectra of vitamin B12' coenzyme B12' and other corrinoids: application of partially-relaxed fourier transform spectroscopy

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Identification of tryptophan resonances in natural abundance carbon-13 nuclear magnetic resonance spectra of proteins. Application of partially relaxed Fourier transform spectroscopy

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Participation of the protein ligands in the folding of cytochrome c

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Spin-lattice relaxation times of imidazole protons and their relevance to NMR studies of proteins

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Electrostatic effects in myoglobin. Hydrogen ion equilibria in sperm whale ferrimyoglobin.

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Electrostatic effects in myoglobin. pH and ionic strength variations of ionization equilibria for individual groups in sperm whale ferrimyoglobin.

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21 December 2022

Brookhaven symposia in biology

78

15

216

author name string

Kendrew

publication date

1962

1 reference

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MAGNETIC RESONANCE STUDIES OF METAL ACTIVATION OF ENZYMIC REACTIONS OF NUCLEOTIDES AND OTHER PHOSPHATE SUBSTRATES

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The lanthanide cations as probes in biological systems. Proton relaxation enhancement studies for model systems and lysozyme

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Magnetic resonance study of the Mn 2+ --lysozyme complex

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Mapping of the binding site of N-fluoroacetyl-D-glucosamine and analogues in hen egg lysozyme by 1H and 19F-NMR techniques with Gd(III) and Mn(II) as paramagnetic probes

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The mechanism of water-proton relaxation in enzyme paramagnetic-ion complexes. 1. The Gd(3)-lysozyme complex

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Binding of divalent copper ions to aspartic acid residue 52 in hen egg-white lysozyme

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Structure of Lysozyme: X. On the Structural Role of Tryptophan Residues*

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Europe PubMed Central

15 September 2017

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