Related ArticlesMolecular conformation of porcine amelogenins and its significance in protein-mineral interaction: 1H-NMR photo-CIDNP study.
J Biol Buccale. 1990 Sep;18(3):189-94
Authors: Aoba T, Kawano K, Moreno EC
The present 1H-nmr study was undertaken to investigate the molecular structure of porcine amelogenins in solution using photo-CIDNP (chemically induced dynamic nuclear polarization). The proteins of interest were the parent 25 kD amelogenin consisting of 173 amino acid residues and its degraded products having molecular masses of 23 kD, 20 kD, 13 kD and 5 kD on SDS-PAGE. From the recorded 1H-nmr and photo-CIDNP spectra, it was found that: 1) the Trp161 at the C-terminus of the 25 kD protein showed a stronger photo-CIDNP effect than the other two Trp25,45 at the N-terminus; 2) Tyr residues at the N-terminus of the 25 kD and 20 kD amelogenins gave rise to the strong peak around 6.8 ppm, indicating that at least some of the six Tyr residues are surface residues; and 3) the accessibility of His residues was quite different between the 13 kD fragment and the 25 kD and 20 kD proteins. These results suggest that the hydrophilic segment at the C-terminus is most likely exposed on the molecular surface and that the molecular structure of the amelogenin in solution may change substantially by the cleavage of the segments at the N- and C-termini.
[NMR paper] Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular d
Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Related Articles Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Biopolymers. 2002 Nov 15;65(4):284-98
Authors: Dixon AM, Venable RM, Pastor RW, Bull TE
A peptide fragment from a protein hairpin turn region was modified by addition of isoleucine residues to both ends to enhance binding to lipid micelles; the resulting peptide (I(1)-I(2)-C(3)-N(4)-N(5)-P(6)-H(7)-I(8)-I(9)) contains the core...
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[NMR paper] Molecular mobility of protein in lyophilized formulations linked to the molecular mob
Molecular mobility of protein in lyophilized formulations linked to the molecular mobility of polymer excipients, as determined by high resolution 13C solid-state NMR.
Related Articles Molecular mobility of protein in lyophilized formulations linked to the molecular mobility of polymer excipients, as determined by high resolution 13C solid-state NMR.
Pharm Res. 1999 Oct;16(10):1621-5
Authors: Yoshioka S, Aso Y, Kojima S, Sakurai S, Fujiwara T, Akutsu H
PURPOSE: The mobility of protein molecules in lyophilized protein formulations was compared...
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[NMR paper] Molecular dynamics-derived conformation and intramolecular interaction analysis of th
Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
Related Articles Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
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[NMR paper] Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics si
Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.
Related Articles Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.
Biopolymers. 1995 Oct;36(4):485-95
Authors: Chorev M, Behar V, Yang Q, Rosenblatt M, Mammi S, Maretto S, Pellegrini M, Peggion E
The conformation of two highly potent parathyroid hormone (PTH) antagonists was investigated in water/2,2,2-trifluoroethanol mixtures. The two peptides are derived from the sequence (7-34) of PTH and of...
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[NMR paper] Solution structure of porcine pancreatic procolipase as determined from 1H homonuclea
Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR.
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 Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR.
Eur J Biochem. 1995 Feb 1;227(3):663-72
Authors: Breg JN, Sarda L, Cozzone PJ, Rugani N, Boelens R, Kaptein R
Procolipase is...
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[NMR paper] NMR studies of interactions between inhibitors and porcine pancreatic phospholipase A
NMR studies of interactions between inhibitors and porcine pancreatic phospholipase A2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of interactions between inhibitors and porcine pancreatic phospholipase A2.
Biochimie. 1992 Sep-Oct;74(9-10):859-66
Authors: Peters AR, Dekker N, van den Berg L, Boelens R, Slotboom AJ, de Haas GH, Kaptein R
Two-dimensional NMR studies were performed on the complexes of porcine pancreatic phospholipase A2, bound to a...
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[NMR paper] The NMR structure of the activation domain isolated from porcine procarboxypeptidase
The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
EMBO J. 1991 Jan;10(1):11-5
Authors: Vendrell J, Billeter M, Wider G, Avilés FX, Wüthrich K
The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR...
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T1 and T2 of Mineral oil at 125MHz
I have spent a day with google and pub-med trying to find this value.
Anyone know it?
I am lookig for the T1 and T2 of Pure mineral oil from ALdrich.
Any help would be greatly appreciated.
Molecular conformation of porcine amelogenins and its significance in protein-mineral
Linear Mode
