1H-NMR assignments have been defined for the aromatic-ring protons of the bovine, guinea pig and human variants of alpha-lactalbumin. Spin-system networks were identified by means of double-quantum-filtered two-dimensional J-correlated spectroscopy and two-dimensional relayed coherence spectroscopy data. Analysis of two-dimensional nuclear-Overhauser-enhancement spectroscopy data of the proteins indicated that in each case two clusters of aromatic residues exist. The two clusters are also evident in the crystal structure of the human protein, and this evidence, in conjunction with sequence differences between the three proteins, permitted sequence-specific assignments to be made for the majority of aromatic residues. Remaining ambiguities in the assignments could be resolved by analysis of photochemically induced dynamic nuclear polarization (PCIDNP) effects. Comparison of the PCIDNP spectra of the three proteins indicated the presence of only minor differences in the surface exposure of conserved aromatic residues. Taken together, these results indicate that the environments of the conserved aromatic residues in bovine, guinea pig and human alpha-lactalbumin in solution are very similar to each other, and that the solution and the crystal forms of at least the human protein are similar.
Defects in Doped LaGaO3 Anionic Conductors: Linking NMR Spectral Features, Local Environments, and Defect Thermodynamics
Defects in Doped LaGaO3 Anionic Conductors: Linking NMR Spectral Features, Local Environments, and Defect Thermodynamics
Fre?de?ric Blanc, Derek S. Middlemiss, Zhehong Gan and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2053557/aop/images/medium/ja-2011-053557_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2053557
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http://feeds.feedburner.com/~r/acs/jacsat/~4/R27buwz0vpI
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10-14-2011 08:08 AM
Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation
Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation
Abstract The measurements of cross-correlated relaxation rates between HNâ??N and Cβâ??Cγ intraresidual and sequential dipolar interactions is demonstrated in ASN, ASP and aromatic residues. The experiment can be used for deuterated samples and no additional knowledge such as Karplus parametrizations is required for the analysis. The data constitutes a new type of information since no other method relates the Cβâ??Cγ bond to HNâ??N. Using this method the dominant populations of rotamer...
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01-09-2011 12:46 PM
[NMR paper] NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
Related Articles NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
J Am Chem Soc. 2005 Sep 14;127(36):12620-6
Authors: Torizawa T, Ono AM, Terauchi T, Kainosho M
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/15N-labeled...
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12-01-2010 06:56 PM
Linking Local Environments and Hyperfine Shifts: A Combined Experimental and Theoreti
Linking Local Environments and Hyperfine Shifts: A Combined Experimental and Theoretical 31P and 7Li Solid-State NMR Study of Paramagnetic Fe(III) Phosphates
Jongsik Kim, Derek S. Middlemiss, Natasha A. Chernova, Ben Y. X. Zhu, Christian Masquelier and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja102678r/aop/images/medium/ja-2010-02678r_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja102678r
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11-17-2010 06:08 PM
[NMR paper] NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexe
NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexes: implications for solution structure and for function.
Related Articles NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexes: implications for solution structure and for function.
Biochemistry. 1995 Feb 21;34(7):2137-47
Authors: Breslow E, Sardana V, Deeb R, Barbar E, Peyton DH
The NMR behavior of the aromatic protons of bovine neurophysin-I and its complexes was interpreted with reference to the 2.8 A crystal structure of...
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08-22-2010 03:41 AM
[NMR paper] 1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions wi
1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions with heparin.
Related Articles 1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions with heparin.
Biochim Biophys Acta. 1991 Jun 24;1078(2):208-18
Authors: Talpas CJ, Walz DA, Lee L
1H-NMR spectroscopy has been used to assign and to characterize the two histidine C2H resonances of the heparin binding protein, bovine platelet factor 4. One histidine has a pKa value of 6.51 at 27 degrees C; the second histidine exhibits 2 pKa values...
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08-21-2010 11:16 PM
[NMR paper] Sequence-specific 1H NMR assignments and structural characterization of bovine semina
Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Related Articles Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Biochemistry. 1991 Feb 12;30(6):1663-72
Authors: Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M
Sequence-specific resonance assignments for the isolated second or b domain of the bovine seminal fluid protein PDC-109 have been obtained from analysis of two-dimensional 1H...
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[NMR paper] The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei
The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
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 The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
Eur J Biochem. 1990 Aug 17;191(3):659-68
Authors: Birdsall B, Arnold JR, Jimenez-Barbero J,...