Academic literature on the topic 'Proteins Solid state chemistry'
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Journal articles on the topic "Proteins Solid state chemistry"
Derome, Andrew E., and Suzanne Bowden. "Low-temperature solid-state NMR of proteins." Chemical Reviews 91, no. 7 (November 1991): 1307–20. http://dx.doi.org/10.1021/cr00007a001.
Full textTang, Ming, and Dennis Lam. "Paramagnetic solid-state NMR of proteins." Solid State Nuclear Magnetic Resonance 103 (November 2019): 9–16. http://dx.doi.org/10.1016/j.ssnmr.2019.101621.
Full textSmith, S. O., and R. G. Griffin. "High-Resolution Solid-State NMR of Proteins." Annual Review of Physical Chemistry 39, no. 1 (October 1988): 511–35. http://dx.doi.org/10.1146/annurev.pc.39.100188.002455.
Full textOpella, S. J. "Solid-State NMR Structural Studies of Proteins." Annual Review of Physical Chemistry 45, no. 1 (October 1994): 659–83. http://dx.doi.org/10.1146/annurev.pc.45.100194.003303.
Full textHeise, Henrike. "Solid-State NMR Spectroscopy of Amyloid Proteins." ChemBioChem 9, no. 2 (January 25, 2008): 179–89. http://dx.doi.org/10.1002/cbic.200700630.
Full textLange, Adam, and Beat Meier. "Fungal prion proteins studied by solid-state NMR." Comptes Rendus Chimie 11, no. 4-5 (April 2008): 332–39. http://dx.doi.org/10.1016/j.crci.2007.08.014.
Full textHansen, Sara K., Kresten Bertelsen, Berit Paaske, Niels Chr Nielsen, and Thomas Vosegaard. "Solid-state NMR methods for oriented membrane proteins." Progress in Nuclear Magnetic Resonance Spectroscopy 88-89 (August 2015): 48–85. http://dx.doi.org/10.1016/j.pnmrs.2015.05.001.
Full textWylie, Benjamin J., Hoa Q. Do, Collin G. Borcik, and Emily P. Hardy. "Advances in solid-state NMR of membrane proteins." Molecular Physics 114, no. 24 (November 8, 2016): 3598–609. http://dx.doi.org/10.1080/00268976.2016.1252470.
Full textRoehrich, Adrienne, and Gary Drobny. "Solid-State NMR Studies of Biomineralization Peptides and Proteins." Accounts of Chemical Research 46, no. 9 (August 9, 2013): 2136–44. http://dx.doi.org/10.1021/ar300321e.
Full textPikal, Michael J., Daniel Rigsbee, and Michael J. Akers. "Solid state chemistry of proteins IV. what is the meaning of thermal denaturation in freeze dried proteins?" Journal of Pharmaceutical Sciences 98, no. 4 (April 2009): 1387–99. http://dx.doi.org/10.1002/jps.21517.
Full textDissertations / Theses on the topic "Proteins Solid state chemistry"
Lee, Myungwoon. "Structure and dynamics of membrane proteins from solid-state NMR." Thesis, Massachusetts Institute of Technology, 2018. http://hdl.handle.net/1721.1/120908.
Full textCataloged from PDF version of thesis.
Includes bibliographical references.
Solid-state nuclear magnetic resonance (SSNMR) spectroscopy is an essential tool to elucidate the structure, dynamics, and function of biomolecules. This thesis mainly focuses on the structure determination of the hydrophobic domains for fusion proteins which are involved in membrane fusion between the cell membrane and viral envelope. Although extensive structural studies have been conducted on the soluble ectodomain by crystallography, the structural topologies of the hydrophobic TMD of the fusion proteins have been poorly understood. Here, we introduced SSNMR to investigate the secondary structure and oligomeric states of the TMD of two fusion proteins, PIV5 F and HIV gp41. For the PIV5 TMD, the membrane dependent secondary structure was determined by measuring the chemical shifts: predominant a-helical conformation in the POPC/cholesterol membrane shifts to the [Beta]-strand in the POPE membrane. Using 19F spin diffusion experiments on the fluorinated TMD, we have determined that the TMD forms a trimeric helical bundle. For the HIV gp4l MPER-TMD, we found the presence of a turn between the MPER helix and the TMD helix by measuring intramolecular distances and probing the lipid-peptide and water-peptide interactions. Intermolecular 19F- 19F distances of the fluorinated peptides indicate that the MPER-TMD is a trimeric. In addition to membrane fusion proteins, we have studied the oligomeric structure and the zinc-bound coordination geometry of a de novo designed amyloid fibril that catalyzes ester hydrolysis. By measuring the intermolecular contacts, we determined that peptides form parallel-in- register P-sheets and further assemble into stacked bilayers in an antiparallel orientation. The zinc binding sites were confirmed by the chemical shifts perturbation of histidines with zinc and the specific zinc-bound geometry was identified by measuring intra-residue distances of histidines. We also investigated the effects of cryoprotectants on the spectral resolution of lipid membranes and membrane peptides at low temperature. 13C and 1H MAS spectra of various cryoprotected membranes showed that DMSO provides the best resolution enhancement with the best ice formation retardation at low temperature and DLPE lipid exhibits the excellent resolution.
by Myungwoon Lee.
Ph. D.
Kwon, Byungsu. "Characterization of structure and dynamics of membrane proteins from solid-state NMR." Thesis, Massachusetts Institute of Technology, 2018. http://hdl.handle.net/1721.1/118268.
Full textCataloged from PDF version of thesis.
Includes bibliographical references.
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy is an essential tool for elucidating the structure, dynamics, and function of biomolecules. ssNMR is capable of studying membrane proteins in near-native lipid bilayers and is thus preferred over other biophysical techniques for characterizing the structure and dynamics of membrane proteins. This thesis primarily focuses on the study of the following membrane proteins: 1) the N-terminal ectodomain and C-terminal cytoplasmic domain of influenza A virus M2 and 2) HIV-1 glycoprotein gp4l membrane-proximal external region and transmembrane domain (MPER-TMD) in a near native membrane environment. The cytoplasmic domain of M2 is necessary for membrane scission and virus shedding. The M2(22-71) construct shows random-coil chemical shifts, large motional amplitudes, and a membrane surface-bound location with close proximity to water, indicating the post-amphipathic helix (AH) cytoplasmic domain is a dynamic random coil near the membrane surface. The influenza M2 ectodomain contains highly conserved epitopes but its structure is largely unknown. The M2(1-49) construct containing both the ectodomain and transmembrane domain exhibits an entirely unstructured ectodomain with a motional gradient in which the motion is slower for residues near the TM domain, which attributed to the formation of a tighter helical bundle in the presence of drug that should cause the more tightened C-terminal ectodomain, thereby slowing its local motions. HIV-1 virus gp4l is directly involved in virus-cell membrane fusion. However, the structural topologies of the gp4l MPER-TMD are still controversial and the biologically-relevant intrinsic conformational state of MPER has not yet been determined. In order to obtain near native structural information of gp4l, we have studied gp41 (665-704) and found a primarily a-helical conformation, membrane-anchored trimeric TMD and water-exposed membrane surface-bound MPER. Intra- and intermolecular distances measured using ¹⁹C-¹⁹F REDOR and ¹⁹F-¹⁹F CODEX revealed that MPER-TMD has a significant kink between MPER and TMD, which has aided a deeper understanding of the HIV virus entry mechanism and the design of vaccines.
by Byungsu Kwon.
Ph. D. in Physical Chemistry
Sengupta, Ishita. "Solid State NMR Structural Studies of Proteins Modified with Paramagnetic Tags." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1354321906.
Full textLewandowski, Józef Romuald. "Methodology and applications of high resolution solid-state NMR to structure determination of proteins." Thesis, Massachusetts Institute of Technology, 2008. http://hdl.handle.net/1721.1/45640.
Full textThis electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.
Vita.
Includes bibliographical references.
A number of methodological developments and applications of solid-state NMR for assignment and high resolution structure determination of microcrystalline proteins and amyloid fibrils are presented. Magic angle spinning spectroscopy on uniformly and selectively "C and '5N labeled samples is performed at magnetic fields from 11.7 to 21.1 T and spinning frequencies from 9 to 65 kHz.Dynamic Nuclear Polarization on nanocrystals of amyloidogenic peptide GNNQQNY is presented demonstrating that 'H-'H spin diffusion can efficiently transfer the enhanced polarization across the solute that is not in an intimate contact with the polarizing agent.An improved theoretical treatment of Rotational Resonance Width (R2W) experiments and its application to determination of precise 13C-13C distance is presented. A general theory of second averaging in modulation frame for designing solid-state NMR experiments is introduced and discussed in the context of two methods: Cosine Modulated Rotary Resonance (CMpRR) for performing a broadband double-quantum 13C-13C recoupling without the need for additional 'H decoupling and Cosine Modulated recoupling with Chemical Shift reintroduction (COMICS) that provides a general frequency selective method for measuring precise 13C-13C distances in uniformly labeled solids. Cosine Modulated Adiabatic Recoupling (CMAR) - an adiabatic extension of the CMpRR, that is particularly robust with respect to rf inhomogeneity, is also introduced. A number of applications CMpRR at 21.1 T to proteins with varying degrees of macroscopic order are presented. A second order Third Spin Assisted Recoupling (TSAR) mechanism is introduced and discussed in detail. The heteronuclear TSAR - Proton Assisted Insensitive Nuclei Cross-Polarization (PAIN-CP) and homonuclear Proton Assisted Recoupling (PAR) yield long distance 13C_1-N, 3C-_13C and 15N- 5N restraints in uniformly labeled systems with spinning frequencies up to 65 kHz that are used for protein structure calculation. Structure, dynamics and polymorphism of amyloidogenic peptide GNNQQNY from the yeast protein sup35p are investigated. Finally, PAIN-CP and '3C-13C PAR are used for high resolution de novo structure determination of 10.4 kDa Crh protein dimer.
by Józef Romuald Lewandowski.
Ph.D.
Bajaj, Vikram Singh. "Dynamic nuclear polarization in biomolecular solid state NMR : methods and applications in peptides and membrane proteins." Thesis, Massachusetts Institute of Technology, 2007. http://hdl.handle.net/1721.1/40874.
Full textIncludes bibliographical references.
Solid state NMR can probe structure and dynamics on length scales from the atomic to the supramolecular. However, low sensitivity limits its application in macromolecules. NMR sensitivity can be improved by dynamic nuclear polarization (DNP), in which electron polarization is transferred to nuclei. We present applications of magic angle spinning NMR that demonstrate its utility for the determination of structure at atomic resolution. We then present new techniques and instrumentation for DNP that permit these methods to be applied to larger systems such as membrane proteins. These applications rest on several advances in instrumentation: millimeter-wave sources and conduits of power to the sample; low-temperature MAS probes incorporating millimeter-wave transmission; cryogenics and pneumatic control systems. We describe a 380 MHz DNP spectrometer incorporating a 250 GHz gyrotron oscillator and present the theory and operation of a 460 GHz gyrotron at the second harmonic of electron cyclotron resonance. We have applied DNP to study trapped photo cycle intermediates of the archael membrane protein bacteriorhodopsin, a light-driven transmembrane ion pump.
(cont.) We have observed the K photointermediate for the first time by NMR and found unexpected conformational heterogeneity in the L intermediate. With multidimensional correlation spectroscopy, we have assigned active site resonances in conformational mixtures of photointermediates of [U-13C,'SN]-bR with high sensitivity. By using non-linear sampling of indirect dimensions, we have observed transient product of K accumulation. We present frequency-selective experiments for amino acid-selective assignments and the measurement of heteronuclear distances and torsion angles in [U-13C, N]-bR and discuss the relevance of these results to its photocycle. In addition, we describe several applications of solid state NMR, including a study of dynamic and structural phase transitions in peptides and proteins near the canonical glass transition temperature. We present resonance width experiments that can be used to measure homonuclear and heteronuclear dipolar couplings in uniformly labeled solids.
(cont.) Finally, we discuss applications to amyloid fibrils, which are protein aggregates that are implicated in diseases of protein misfolding. We report the atomic resolution structure of the disease-associated L 111M mutant of TTR105-115 in an amyloid fibril, and information about the supramolecular structure of fibrils from WT TTRos05115.
by Vikram Singh Bajaj.
Ph.D.
Bower, Peter Velling. "Solid state nuclear magnetic resonance techniques for determining structure in proteins and peptides /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8663.
Full textJaroniec, Christopher P. "Solid state nuclear magnetic resonance methodology and applications to structure determination of peptides, proteins and amyloid fibrils." Thesis, Massachusetts Institute of Technology, 2003. http://hdl.handle.net/1721.1/16914.
Full textVita.
Includes bibliographical references.
This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.
Several methodological developments and applications of multidimensional solid-state nuclear magnetic resonance to biomolecular structure determination are presented. Studies are performed in uniformly 3C, 15N isotope labeled samples with magic-angle spinning for optimal resolution and sensitivity. Frequency selective rotational-echo double-resonance (FSR) and three-dimensional transferred-echo double-resonance (3D TEDOR) methods for carbon-nitrogen distance measurements in (U-'3C,S5N)-labeled peptides and proteins are described. FSR employs frequency selective Gaussian pulses in combination with broadband REDOR recoupling to measure dipolar couplings based on the isotropic chemical shifts of the selected 13C-15N spin pairs. The experiment is demonstrated in model peptides, N-acetyl-L-Val-L-Leu and N-formyl-L-Met-L-Leu-L-Phe, where multiple distances in the 3-6 A range are determined with high precision, and in a membrane protein, bacteriorhodopsin, where the distances between aspartic acids Asp-85 and Asp-212 and the retinal Schiff base nitrogen are measured in the active site. The 3D TEDOR methods employ 13C and 15N chemical shift dimensions for site-specific resolution and encode the distance information in the buildup of cross-peak intensities, allowing multiple distances to be measured simultaneously. The methods are demonstrated in N-acetyl-L-Val-L-Leu and N-formyl-L-Met-L-Leu-L-Phe, where 20 and 26 distances up to 6 A are determined, respectively. The molecular conformation of peptide fragment 105-115 of transthyretin in an amyloid fibril is investigated.
(cont.) Complete sequence-specific 13C and 15N backbone and side- chain resonance assignments are obtained using two-dimensional 13C-13C and 15N-13C-3C chemical shift correlation experiments. Backbone torsion angles are measured directly using three-dimensional dipolar-chemical shift correlation experiments, which report on the relative orientations of 3C-15N, 3C-1H and 15N-'H dipolar tensors, and intramolecular 13C-15N distances in the 3-5 A range are determined using 3D TEDOR, resulting in about 60 constraints on the peptide structure. An atomic-resolution structure of the peptide consistent with the NMR constraints is calculated using simulated annealing molecular dynamics, and the results indicate that the peptide adopts an extended β-strand conformation in the fibril.
by Christopher Peter Jaroniec.
Ph.D.
Lamley, Jonathan M. "Methods for the determination of the structures and dynamics of proteins by solid-state NMR spectroscopy." Thesis, University of Warwick, 2015. http://wrap.warwick.ac.uk/78994/.
Full textJayasinha, Arachchige Rajith Madushanka. "Development of New Paramagnetic Tags for Solid-State NMR Structural Studies of Natively Diamagnetic Proteins." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1388416184.
Full textMayrhofer, Rebecca Maria. "Applications of DNP and solid-state NMR for protein structure determination." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/58201.
Full textVita. Cataloged from PDF version of thesis.
Includes bibliographical references.
Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments.
by Rebecca Maria Mayrhofer.
S.M.
Books on the topic "Proteins Solid state chemistry"
Chakrabarty, D. K. Solid state chemistry. New Delhi: New age international publishers, 2005.
Find full textWold, Aaron, and Kirby Dwight. Solid State Chemistry. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1476-9.
Full textSmart, Lesley, and Elaine Moore. Solid State Chemistry. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-6830-2.
Full textMoore, Elaine A., and Lesley E. Smart. Solid State Chemistry. Fifth edition. | Boca Raton : CRC Press, [2021]: CRC Press, 2020. http://dx.doi.org/10.1201/9780429027284.
Full textR, West Anthony, ed. Basic solid state chemistry. Chichester [West Sussex]: Wiley, 1988.
Find full textChan, Jerry C. C. Solid State NMR. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2012.
Find full textElaine, Moore, ed. Solid state chemistry: An introduction. London: Chapman & Hall, 1992.
Find full textBook chapters on the topic "Proteins Solid state chemistry"
Müller, Henrik, Manuel Etzkorn, and Henrike Heise. "Solid-State NMR Spectroscopy of Proteins." In Topics in Current Chemistry, 121–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/128_2012_417.
Full textZhao, Xin. "Protein Structure Determination by Solid-State NMR." In Topics in Current Chemistry, 187–213. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/128_2011_287.
Full textFahlman, Bradley D. "Solid-State Chemistry." In Materials Chemistry, 13–85. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6120-2_2.
Full textFahlman, Bradley D. "Solid-State Chemistry." In Materials Chemistry, 23–169. Dordrecht: Springer Netherlands, 2018. http://dx.doi.org/10.1007/978-94-024-1255-0_2.
Full textFahlman, Bradley D. "Solid-State Chemistry." In Materials Chemistry, 13–156. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0693-4_2.
Full textCatlow, C. R. A., R. M. Barrer, and I. S. Kerr. "Solid state chemistry." In 100 Years of Physical Chemistry, 339–50. Cambridge: Royal Society of Chemistry, 2007. http://dx.doi.org/10.1039/9781847550002-00339.
Full textHickey, Anthony J., and Stefano Giovagnoli. "Solid-State Chemistry." In AAPS Introductions in the Pharmaceutical Sciences, 5–10. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-91220-2_2.
Full textKoltzenburg, Sebastian, Michael Maskos, and Oskar Nuyken. "Polymers in Solid State." In Polymer Chemistry, 93–103. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49279-6_4.
Full textPyykkö, P. "Solid-State Theory." In Lecture Notes in Chemistry, 150–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-93345-5_8.
Full textPyykkö, Pekka. "Solid-State Theory." In Lecture Notes in Chemistry, 170–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-51488-3_8.
Full textConference papers on the topic "Proteins Solid state chemistry"
Cahen, David. "Proteins as "dopable" bio-electronic materials." In SOLID STATE PHYSICS: PROCEEDINGS OF THE 57TH DAE SOLID STATE PHYSICS SYMPOSIUM 2012. AIP, 2013. http://dx.doi.org/10.1063/1.4791551.
Full textBai, Haihua, Chun Li, Hasi Agula, Jirimutu, Jun Wang, and Lili Xing. "Cp‐curve, a Novel 3‐D Graphical Representation of Proteins." In SOLID STATE PHYSICS, PROCEEDINGS OF THE 55TH DAE SOLID STATE PHYSICS SYMPOSIUM 2010. American Institute of Physics, 2007. http://dx.doi.org/10.1063/1.2836145.
Full textChinchalikar, A. J., Sugam Kumar, V. K. Aswal, J. Kohlbrecher, and A. G. Wagh. "SANS study of understanding mechanism of cold gelation of globular proteins." In SOLID STATE PHYSICS: Proceedings of the 58th DAE Solid State Physics Symposium 2013. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4872538.
Full textZharikov, E. V. "CHROMIUM-DOPED GARNET HOSTS: CRYSTAL CHEMISTRY DEVELOPMENT AND PROPERTIES." In Advanced Solid State Lasers. Washington, D.C.: OSA, 1986. http://dx.doi.org/10.1364/assl.1986.tha1.
Full textHsieh, H. C., M. M. Rahman, T. C. Shen, and H. Kim. "GROWTH OF CARBON NANOTUBES DIRECTLY FROM NATURAL PROTEINS." In 2012 Solid-State, Actuators, and Microsystems Workshop. San Diego: Transducer Research Foundation, 2012. http://dx.doi.org/10.31438/trf.hh2012.118.
Full textPatil, Supriya Veer, Ashwini Kshirsagar, Deepali D. Andhare, Supriya R. Patade, Govind D. Kulkarni, and K. M. Jadhav. "Synthesis of nanocrystalline nickel ferrite through soft chemistry method: A green chemistry approach using ginger extract." In DAE SOLID STATE PHYSICS SYMPOSIUM 2019. AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0017071.
Full textContera, Sonia Antoranz, Kislon Voitchovsky, Hilary Hamnett, Chandra S. Ramanujan, Nashville Toledo, Vincent Lemaitre, Maurits de Planque, et al. "Bionanotechnology with Membrane Proteins: Mechanics and Electronics." In 2005 International Conference on Solid State Devices and Materials. The Japan Society of Applied Physics, 2005. http://dx.doi.org/10.7567/ssdm.2005.h-5-1.
Full textEmaminejad, S., M. Javanmard, S. Chang, C. Gupta, R. T. Howe, and R. W. Davis. "ELECTRICAL ACTUATION AT NANOSCALE: CONTROLLED ORIENTATION OF PROTEINS DURING IMMOBILIZATION." In 2014 Solid-State, Actuators, and Microsystems Workshop. San Diego: Transducer Research Foundation, 2014. http://dx.doi.org/10.31438/trf.hh2014.86.
Full textDorairaj, R., T. J. Roussel, G. Sumanasekera, P. Sethu, C. M. Klinge, and R. S. Keynton. "CARBON NANOTUBE MEMBRANE IN MICROCHANNEL FOR ELECTROPHORETIC SEPARATION OF PROTEINS." In 2008 Solid-State, Actuators, and Microsystems Workshop. San Diego: Transducer Research Foundation, 2008. http://dx.doi.org/10.31438/trf.hh2008.97.
Full textToner, Brandy M., Brandi Cron, Colleen Hoffman, Sarah L. Nicholas, and Brandy Stewart. "Solid-State Chemistry of Near-Field Hydrothermal Particles." In Goldschmidt2020. Geochemical Society, 2020. http://dx.doi.org/10.46427/gold2020.2610.
Full textReports on the topic "Proteins Solid state chemistry"
Bernhard, W. Solid state radiation chemistry of the DNA backbone. Office of Scientific and Technical Information (OSTI), September 1989. http://dx.doi.org/10.2172/5430309.
Full textHeller, Jonathan. Solid state nuclear magnetic resonance studies of prion peptides and proteins. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/6428.
Full textCosman, M., A. T. Tran, J. Ulloa, and R. S. Maxwell. Development of Solid State NMR Methods for the Structural Characterization of Membrane Proteins: Applications to Understand Multiple Sclerosis. Office of Scientific and Technical Information (OSTI), March 2003. http://dx.doi.org/10.2172/15007469.
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