Related Articles13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocular lenses.
Exp Eye Res. 1993 Mar;56(3):305-16
Authors: Rydzewski JM, Wang SX, Stevens A, Serdahl C, Schleich T
The motional dynamics of lens proteins were studied by two 13C nuclear magnetic resonance (NMR) techniques sensitive to molecular motion to define the effect of lens water content on the presence of solid-like protein domains in ocular lenses from bovine (juvenile and adult), human, rat, and chicken eyes. The solid state 13C NMR technique of proton dipolar decoupling was used to study slow (solid-like) motions (correlation time, tau o > or = 10 microseconds), whereas for intermediate (mobile) protein, rotational reorientational motion (tau o range of 1-500 nsec) the 13C off-resonance rotating frame spin-lattice relaxation technique was employed. 13C NMR studies of calf lens cortical and nuclear homogenates indicated a reversible loss of lens protein motional freedom with decreasing water content. Values of 6% and 63% solid-like protein contents were obtained for native cortical and nuclear calf lens homogenates, respectively. At equivalent total protein concentrations cortical and nuclear calf lens homogenates exhibited essentially the same solid-like (motionally restricted) protein content. Lens protein rotational correlation times determined by off-resonance rotating frame spin-lattice relaxation measurements were consistent with lens protein aggregation. The solid-like protein content of the bovine nuclear lens region was observed to increase with age, whereas no significant change was detected for the cortex. Across lens species an inverse correlation between the percentage of solid-like protein content and water content was observed. Very broad 13C NMR resonances, even in the presence of proton dipolar decoupling, were observed for the lens proteins present in the cataractous human lens, indicating the presence of highly aggregated protein species. The occurrence of solid-like protein domains in lens tissue has implications for the interpretation of proton nuclear magnetic resonance dispersion (NMRD) measurements of lens homogenates and for proton magnetization transfer contrast enhanced magnetic resonance imaging of lens. Solid-like protein domains may play a protective role in the maintenance of lens transparency by minimizing enhanced refractive index fluctuations created by protein packing defects resulting from post-translational modification.
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Abstract Temperature-dependence of protein dynamics can provide information on details of the free energy landscape by probing the characteristics of the potential responsible for the fluctuations. We have investigated the temperature-dependence of picosecond to nanosecond backbone dynamics at carbonyl carbon sites in chicken villin headpiece subdomain protein using a combination of three NMR relaxation rates: 13Cā?² longitudinal rate, and two cross-correlated rates involving dipolar and...
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[NMR paper] Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxatio
Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Related Articles Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Protein Sci. 1998 Mar;7(3):720-9
Authors: Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH
Structurally characterizing partially folded peptides is problematic given the nature of their transient conformational states. 13C-NMR relaxation data can provide information on the geometry of bond rotations, motional restrictions, and correlated bond rotations...
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11-17-2010 11:06 PM
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...
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09-10-2010 11:53 PM
[NMR paper] Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
Related Articles Cadmium-113 NMR studies of bovine and human alpha-lactalbumin and equine lysozyme.
J Biochem. 1995 Mar;117(3):623-8
Authors: Aramini JM, Hiraoki T, Ke Y, Nitta K, Vogel HJ
The high-affinity calcium-binding sites of bovine and human alpha-lactalbumin as well as equine lysozyme were analyzed by 113Cd NMR spectroscopy. In the case of equine lysozyme, the addition of isotopically enriched 113Cd2+ results in a signal at delta = -75.9 ppm...
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[NMR paper] Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Related Articles Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Biochemistry. 1994 Mar 22;33(11):3304-11
Authors: Aramini JM, Krygsman PH, Vogel HJ
We have examined the binding of Tl3+ to human serotransferrin and chicken ovotransferrin in the presence of carbonate and oxalate by 205Tl and 13C NMR spectroscopy. With carbonate as the synergistic anion, one observes two 205Tl NMR signals due to the bound metal ion in the two...
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[NMR paper] Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Related Articles Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Biochemistry. 1994 Mar 22;33(11):3304-11
Authors: Aramini JM, Krygsman PH, Vogel HJ
We have examined the binding of Tl3+ to human serotransferrin and chicken ovotransferrin in the presence of carbonate and oxalate by 205Tl and 13C NMR spectroscopy. With carbonate as the synergistic anion, one observes two 205Tl NMR signals due to the bound metal ion in the two...
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08-22-2010 03:33 AM
[NMR paper] Comparative studies of the interaction of human and bovine platelet factor 4 with hep
Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
Related Articles Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
J Protein Chem. 1993 Jun;12(3):303-9
Authors: Talpas CJ, Lee L
The pKa values of His-38 and His-50 of the heparin-binding protein, bovine platelet factor 4, are 5.6 and 6.5, respectively, as determined by 1H NMR spectroscopy. The 1H NMR...
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08-21-2010 11:53 PM
[NMR paper] NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-ma
NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
Related Articles NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
J Biol Chem. 1990 May 5;265(13):7268-72
Authors: Gettins P, Sottrup-Jensen L
NMR and ESR spectroscopies have been used to examine the plasma protease inhibitor pregnancy zone protein (PZP) and its complex with chymotrypsin. The 1H NMR spectrum of PZP shows relatively few sharp resonances, which, by analogy with human alpha...