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High-probability grants
According to our matching algorithm, He Liu is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1997 |
Liu, He |
P41Activity Code Description: Undocumented code - click on the grant title for more information. |
Nmr Structure Determination of Prion Protein @ University of California San Francisco
proteins; nervous system; biomedical resource;
|
0.957 |
1998 — 1999 |
Liu, He |
P41Activity Code Description: Undocumented code - click on the grant title for more information. |
Determination of Solution Structure of Recombinant Syrian Hamster Prion Protein @ University of California San Francisco
Prions cause neurodegenerative diseases in humans and animals. The infectious prions are largely composed of a host encoded glycoprotein denoted PrP-Sc. Limited digestion of PrP-Sc by proteinase K yields an N- terminally truncated polypeptide corresponding primarily to residues 90- 231, which remains infectious when injected into normal healthy animal. We are studying the structure of recombinant Syrian Hamster Prion Protein rPrP(90-231) using multi-dimensional NMR. We use the NMR spectral analysis and database management program (SPARKY) to assign the backbone and sidechain 1H, 13C and 15N resonances of the protein. The assignment for over 3000 NOEs and the management of the data for about 1000 proton resonances are also made using SPARKY. In the structure refinement process, we constantly use molecular graphics (MidasPlus) to check the results of our calculations, and display the NMR constraints with the program noeshow. The interactive process of examining the structure and adding in restraints is heavily dependent on graphics since we have such a great deal of spectral overlap. Finally we use the molecular graphics capabilities of MidasPlus to produce figures for publications and presentations.
|
0.957 |
1999 — 2001 |
Liu, He |
P41Activity Code Description: Undocumented code - click on the grant title for more information. |
Development of Mardigras &Corma @ University of California San Francisco
Inter-proton distances derived from NOE (nuclear Overhauser effect) data are the main structural information obtained from NMR. The focus of my research is to obtain accurate distance constraints from NOE data using complete relaxation matrix method. It has been shown that for high resolution structure determination, it is important that accurate distance constraints are used in the structure calculations. This is particularly true for DNA, DNA-drug complex and RNA, where the number of NMR distance constraints per residue is relatively small. We have developed programs CORMA and MARDIGRAS for the analysis of NOE data using complete relaxation matrix methods. Accurate distance constraints can be obtained by taking into account indirect cross relaxation (spin diffusion) in large spin systems. Distance restraints are determined by adding random errors to NOE intensities using RANDMARDI procedure. Recent development of CORMA and MARDIGRAS involves rewriting the Fortran code in C++, and the interface with Sparky, a graphical NMR software used for display and assignment of multi-dimensional NMR spectra.
|
0.957 |
1999 — 2001 |
Liu, He |
P41Activity Code Description: Undocumented code - click on the grant title for more information. |
Structure Determination of Rprp(90 231) @ University of California San Francisco
We have determined the structure of a recombinant fragment (90-231) of Syrian hamster PrP gene product using 3 dimensional heteronuclear NMR. Prions are infectious particles that cause fatal neurodegenerative disorders in humans and animals, such as scrapie in sheep, mad cow disease, and kuru, Cruetzfeld-Jakob, Gerstmann-Staussler-Scheinker disease, and fatal familial insomnia in humans. The diseases' process is unusual in that it is propagated by the change of the conformation of prion proteins from the normal cellular form (PrPc, predominantly alpha helical) to the abnormal aggregated beta-sheet form (PrP Scrapie). The determination of Prp structure is important for both the understanding of prion diseases, and drug design. We use heteronuclear NMR techniques and the graphical NMR software Sparky to make the resonance assignment and NOE cross peak assignment for the determination of the PrP(90-231) structure. The structure was refined using Xplor/Aria and Amber force field. We use molecular graphics (MidasPlus) to check the results of our calculations, and display the NMR constraints with the program noeshow. The interactive process of examining the structure and adding in restraints is heavily dependent on graphics since we have such a great deal of spectral overlap.
|
0.957 |