Related ArticlesIdentification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy.
Biochemistry. 1990 Jun 19;29(24):5671-6
Authors: Clore GM, Bax A, Wingfield PT, Gronenborn AM
The presence and location of bound internal water molecules in the solution structure of interleukin 1 beta have been investigated by means of three-dimensional 1H rotating-frame Overhauser 1H-15N multiple quantum coherence spectroscopy (ROESY-HMQC). In this experiment through-space rotating-frame Overhauser (ROE) interactions between NH protons and bound water separated by less than or equal to 3.5 A are clearly distinguished from chemical exchange effects, as the cross-peaks for these two processes are of opposite sign. The identification of ROEs between NH protons and water is rendered simple by spreading out the spectrum into a third dimension according to the 15N chemical shift of the directly bonded nitrogen atoms. By this means, the problems that prevent, in all but a very few limited cases, the interpretation, identification, and assignment of ROE peaks between NH protons and water in a 2D 1H-1H ROESY spectrum of a large protein such as interleukin 1 beta, namely, extensive NH chemical shift degeneracy and ROE peaks obscured by much stronger chemical exchange peaks, are completely circumvented. We demonstrate the existence of 15 NH protons that are close to bound water molecules. From an examination of the crystal structure of interleukin 1 beta [Finzel, B. C., Clancy, L. L., Holland, D. R., Muchmore, S. W., Watenpaugh, K. D., & Einspahr, H. M. (1989) J. Mol. Biol. 209, 779-791], the results can be attributed to 11 water molecules that are involved in interactions bridging hydrogen-bonding interactions with backbone amide and carbonyl groups which stabilize the 3-fold pseudosymmetric topology of interleukin 1 beta and thus constitute an integral part of the protein structure in solution.
[NMR paper] NMR solution structure of attractin, a water-borne protein pheromone from the mollusk
NMR solution structure of attractin, a water-borne protein pheromone from the mollusk Aplysia californica.
Related Articles NMR solution structure of attractin, a water-borne protein pheromone from the mollusk Aplysia californica.
Biochemistry. 2003 Aug 26;42(33):9970-9
Authors: Garimella R, Xu Y, Schein CH, Rajarathnam K, Nagle GT, Painter SD, Braun W
Water-borne protein pheromones are essential for coordination of reproductive activities in many marine organisms. In this paper, we describe the first structure of a pheromone protein from a...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.
Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.
Related Articles Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.
J Mol Biol. 2002 Dec 13;324(5):1003-14
Authors: Inman KG, Yang R, Rustandi RR, Miller KE, Baldisseri DM, Weber DJ
The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-workers...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] NMR identification of hydrophobic cavities with low water occupancies in protein stru
NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Related Articles NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Nat Struct Biol. 1997 May;4(5):396-404
Authors: Otting G, Liepinsh E, Halle B, Frey U
Magnetization transfer through dipole-dipole interactions (nuclear Overhauser effects, NOEs) between water protons and the protons lining two small hydrophobic cavities in hen egg-white lysozyme demonstrates...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] NMR identification of hydrophobic cavities with low water occupancies in protein stru
NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Related Articles NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Nat Struct Biol. 1997 May;4(5):396-404
Authors: Otting G, Liepinsh E, Halle B, Frey U
Magnetization transfer through dipole-dipole interactions (nuclear Overhauser effects, NOEs) between water protons and the protons lining two small hydrophobic cavities in hen egg-white lysozyme demonstrates...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Related Articles Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
J Biomol NMR. 1995 Jun;5(4):415-9
Authors: Cistola DP, Hall KB
A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines 19F-detected heteronuclear Overhauser and exchange spectroscopy (HOESY) with site-specific 19F substitution. The model system employed was intestinal fatty acid-binding protein complexed with...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] Native like structure and stability of apo AI in a n-propanol/water solution as deter
Native like structure and stability of apo AI in a n-propanol/water solution as determined by 13C NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Native like structure and stability of apo AI in a n-propanol/water solution as determined by 13C NMR.
FEBS Lett. 1995 Mar 13;361(1):29-34
Authors: Leroy A, Lippens G, Wieruszeski JM, Parra HJ, Fruchart JC
To elucidate the molecular details of the conformation of apolipoprotein AI (apo AI), we have developed an approach...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Related Articles The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Biochemistry. 1991 Jul 2;30(26):6563-74
Authors: Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K
Cyclosporin A bound to the presumed receptor protein cyclophilin was studied in aqueous solution at pH 6.0 by nuclear magnetic resonance spectroscopy using uniform 15N- or 13C-labeling of cyclosporin A and heteronuclear spectral editing techniques....
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Related Articles The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Biochemistry. 1991 Jul 2;30(26):6563-74
Authors: Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K
Cyclosporin A bound to the presumed receptor protein cyclophilin was studied in aqueous solution at pH 6.0 by nuclear magnetic resonance spectroscopy using uniform 15N- or 13C-labeling of cyclosporin A and heteronuclear spectral editing techniques....
Identification and localization of bound internal water in the solution structure of
Linear Mode
