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Relevant bibliographies by topics / Structure and Dynamics of Peptides by NMR Spectroscopy

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Academic literature on the topic 'Structure and Dynamics of Peptides by NMR Spectroscopy'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

1

Siminovitch, David J. "Solid-state NMR studies of proteins: the view from static 2H NMR experiments." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 411–22. http://dx.doi.org/10.1139/o98-054.

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The application of solid-state 2H NMR spectroscopy to the study of protein and peptide structure and dynamics is reviewed. The advantages of solid-state NMR for the study of proteins are considered, and the particular advantages of solid-state 2H NMR are summarized. Examples of work on the integral membrane protein bacteriorhodopsin, and the membrane peptide gramicidin, are used to highlight the major achievements of the 2H NMR technique. These examples demonstrate that through the use of oriented samples, it is possible to obtain both structural and dynamic information simultaneously.Key words: solid-state NMR, 2H NMR, membrane peptides, membrane proteins, oriented bilayers.

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Ader, C., R. Schneider, K. Seidel, M. Etzkorn, and M. Baldus. "Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 991–95. http://dx.doi.org/10.1042/bst0350991.

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ssNMR (solid-state NMR) spectroscopy provides increasing possibilities to study the structural and dynamic aspects of biological membranes. Here, we review recent ssNMR experiments that are based on MAS (magic angle spinning) and that provide insight into the structure and dynamics of membrane systems at the atomic level. Such methods can be used to study membrane architecture, domain formation or molecular complexation in a way that is highly complementary to other biophysical methods such as imaging or calorimetry.

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Hong, Mei. "Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy." Journal of Physical Chemistry B 111, no. 35 (September 2007): 10340–51. http://dx.doi.org/10.1021/jp073652j.

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POLYANSKY, ANTON A., PAVEL E. VOLYNSKY, and ROMAN G. EFREMOV. "COMPUTER SIMULATIONS OF MEMBRANE-LYTIC PEPTIDES: PERSPECTIVES IN DRUG DESIGN." Journal of Bioinformatics and Computational Biology 05, no. 02b (April 2007): 611–26. http://dx.doi.org/10.1142/s0219720007002783.

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Structure activity relationships were investigated for membrane-lytic peptides (MLP) Ltc1 and Ltc2a from the latarcin family. The peptides were studied via long-term molecular dynamics (MD) simulations in different membrane environments (detergent micelles, mixed lipid bilayers mimiking eukaryotic and bacterial membranes). The calculated structure of Ltc2a in sodium dodecyl sulfate micelle agrees well with the data obtained by 1H-NMR spectroscopy. This validates the applied modeling approach. The binding mode of MLPs is governed by several factors: (i) the membrane surface curvature; (ii) the conformational plasticity and hydrophobic organization of the peptide, which depend on the arrangement of charged, non-polar and helix-breaking residues in the amino acid sequence. In contrast to Ltc1, insertion of Ltc2a into model membranes induces significant changes in dynamic behavior of lipids in the contact region. Such a prominent membrane destabilization correlates with high membrane-lytic activity of Ltc2a. In all cases the "membrane response" has a local character and is caused by formation of specific peptide-lipid contacts. Results of MD simulations of Ltc2a in model membranes were used to develop a number of its analogs with predefined activity.

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BUCK, MATTHIAS. "Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins." Quarterly Reviews of Biophysics 31, no. 3 (August 1998): 297–355. http://dx.doi.org/10.1017/s003358359800345x.

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Alcohol based cosolvents, such as trifluoroethanol (TFE) have been used for many decades to denature proteins and to stabilize structures in peptides. Nuclear magnetic resonance spectroscopy and site directed mutagenesis have recently made it possible to characterize the effects of TFE and of other alcohols on polypeptide structure and dynamics at high resolution. This review examines such studies, particularly of hen lysozyme and β-lactoglobulin. It presents an overview of what has been learnt about conformational preferences of the polypeptide chain, the interactions that stabilize structures and the nature of the denatured states. The effect of TFE on transition states and on the pathways of protein folding and unfolding are also reviewed. Despite considerable progress there is as yet no single mechanism that accounts for all of the effects TFE and related cosolvents have on polypeptide conformation. However, a number of critical questions are beginning to be answered. Studies with alcohols such as TFE, and ‘cosolvent engineering’ in general, have become valuable tools for probing biomolecular structure, function and dynamics.1. COSOLVENTS: OLD HAT? 2982. HOW DOES TFE WORK? 2992.1 Effect on hydrogen bonding 3002.2 Effect on non-polar sidechains 3012.3 Effect on solvent structure 3023. EFFECTS OF TFE ON (UN-)FOLDING TRANSITIONS 3033.1 Pretransition 3033.2 Transition 3043.3 Posttransition 3053.4 Far UV CD spectroscopic detection of structure 3063.5 Effect with temperature 3063.6 Effect with additional denaturants 3064. THERMODYNAMIC PARAMETERS FROM STRUCTURAL TRANSITIONS OF PEPTIDES AND PROTEINS IN TFE 3075. ADVANCES IN NMR SPECTROSCOPY 3105.1 Chemical shifts 3105.2 3[Jscr ]HNHαcoupling constants 3115.3 Amide hydrogen exchange 3125.4 Nuclear Overhauser Effects (NOEs) 3126. α-HELIX – EVERYWHERE? 3136.1 Intrinsic helix propensity equals helix content? 3136.2 A helix propensity scale for the amino acids in TFE 3146.3 Capping motifs and stop signals 3156.4 Limits and population of helices as seen by CD and NMR 3167. TURNS 3178. β-HAIRPINS AND SHEETS 3179. ‘CLUSTERS’ OF SIDECHAINS 32010. THE TFE DENATURED STATE OF β-LACTOGLOBULIN 32111. THE TFE DENATURED STATE OF HEN LYSOZYME 32412. TERTIARY STRUCTURE, DISULPHIDES, DYNAMICS AND COMPACTNESS 32713. PROSPECTS FOR STRUCTURE CALCULATION 32814. EFFECT OF TFE ON QUATERNARY STRUCTURE 32915. EFFECT ON TFE ON UN- AND REFOLDING KINETICS 33016. OTHER USES 33616.1 Mimicking membranes and protein receptors 33616.2 Solubilizing peptides and proteins 33616.3 Cosolvents as helpers for protein folding? 33816.4 Modifying protein dynamics and catalysis 33816.5 Effects on nucleic acids 33916.6 Effects on lipid bilayers and micelles 33916.7 Future applications 33917. CONCLUSIONS: TFE – WHAT IS IT GOOD FOR? 34018. ACKNOWLEDGMENTS 34019. REFERENCES 340

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Krishnan, V. V., Timothy Bentley, Alina Xiong, and Kalyani Maitra. "Conformational Ensembles by NMR and MD Simulations in Model Heptapeptides with Select Tri-Peptide Motifs." International Journal of Molecular Sciences 22, no. 3 (January 29, 2021): 1364. http://dx.doi.org/10.3390/ijms22031364.

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Both nuclear magnetic resonance (NMR) and molecular dynamics (MD) simulations are routinely used in understanding the conformational space sampled by peptides in the solution state. To investigate the role of single-residue change in the ensemble of conformations sampled by a set of heptapeptides, AEVXEVG with X = L, F, A, or G, comprehensive NMR, and MD simulations were performed. The rationale for selecting the particular model peptides is based on the high variability in the occurrence of tri-peptide E*L between the transmembrane β-barrel (TMB) than in globular proteins. The ensemble of conformations sampled by E*L was compared between the three sets of ensembles derived from NMR spectroscopy, MD simulations with explicit solvent, and the random coil conformations. In addition to the estimation of global determinants such as the radius of gyration of a large sample of structures, the ensembles were analyzed using principal component analysis (PCA). In general, the results suggest that the -EVL- peptide indeed adopts a conformational preference that is distinctly different not only from a random distribution but also from other peptides studied here. The relatively straightforward approach presented herein could help understand the conformational preferences of small peptides in the solution state.

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Jobin, Marie-Lise, Lydie Vamparys, Romain Deniau, Axelle Grélard, Cameron Mackereth, Patrick Fuchs, and Isabel Alves. "Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide." International Journal of Molecular Sciences 20, no. 18 (September 9, 2019): 4441. http://dx.doi.org/10.3390/ijms20184441.

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Cell-penetrating peptides (CPPs) are short peptides that can translocate and transport cargoes into the intracellular milieu by crossing biological membranes. The mode of interaction and internalization of cell-penetrating peptides has long been controversial. While their interaction with anionic membranes is quite well understood, the insertion and behavior of CPPs in zwitterionic membranes, a major lipid component of eukaryotic cell membranes, is poorly studied. Herein, we investigated the membrane insertion of RW16 into zwitterionic membranes, a versatile CPP that also presents antibacterial and antitumor activities. Using complementary approaches, including NMR spectroscopy, fluorescence spectroscopy, circular dichroism, and molecular dynamic simulations, we determined the high-resolution structure of RW16 and measured its membrane insertion and orientation properties into zwitterionic membranes. Altogether, these results contribute to explaining the versatile properties of this peptide toward zwitterionic lipids.

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Sinelnikova, Anna, and David van der Spoel. "NMR refinement and peptide folding using the GROMACS software." Journal of Biomolecular NMR 75, no. 4-5 (March 28, 2021): 143–49. http://dx.doi.org/10.1007/s10858-021-00363-z.

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AbstractNuclear magnetic resonance spectroscopy is used routinely for studying the three-dimensional structures and dynamics of proteins and nucleic acids. Structure determination is usually done by adding restraints based upon NMR data to a classical energy function and performing restrained molecular simulations. Here we report on the implementation of a script to extract NMR restraints from a NMR-STAR file and export it to the GROMACS software. With this package it is possible to model distance restraints, dihedral restraints and orientation restraints. The output from the script is validated by performing simulations with and without restraints, including the ab initio refinement of one peptide.

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Bechinger, Burkhard. "The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy." Biochimica et Biophysica Acta (BBA) - Biomembranes 1462, no. 1-2 (December 1999): 157–83. http://dx.doi.org/10.1016/s0005-2736(99)00205-9.

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O’Connor, Casey, Kate L. White, Nathalie Doncescu, Tatiana Didenko, Bryan L. Roth, Georges Czaplicki, Raymond C. Stevens, Kurt Wüthrich, and Alain Milon. "NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor." Proceedings of the National Academy of Sciences 112, no. 38 (September 8, 2015): 11852–57. http://dx.doi.org/10.1073/pnas.1510117112.

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The structure of the dynorphin (1–13) peptide (dynorphin) bound to the human kappa opioid receptor (KOR) has been determined by liquid-state NMR spectroscopy. 1H and 15N chemical shift variations indicated that free and bound peptide is in fast exchange in solutions containing 1 mM dynorphin and 0.01 mM KOR. Radioligand binding indicated an intermediate-affinity interaction, with a Kd of ∼200 nM. Transferred nuclear Overhauser enhancement spectroscopy was used to determine the structure of bound dynorphin. The N-terminal opioid signature, YGGF, was observed to be flexibly disordered, the central part of the peptide from L5 to R9 to form a helical turn, and the C-terminal segment from P10 to K13 to be flexibly disordered in this intermediate-affinity bound state. Combining molecular modeling with NMR provided an initial framework for understanding multistep activation of a G protein-coupled receptor by its cognate peptide ligand.

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Dissertations / Theses on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

1

Tengel, Tobias. "Studies of protein structure, dynamics and protein-ligand interactions using NMR spectroscopy." Doctoral thesis, Umeå : Univ, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1472.

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Amero, Carlos D. "Protein Function Study by NMR Spectroscopy." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1205431343.

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3

Debelouchina, Galia Tzvetanova. "Amyloid fibril structure of peptides and proteins by magic angle spinning NMR spectroscopy and dynamic nuclear polarization." Thesis, Massachusetts Institute of Technology, 2011. http://hdl.handle.net/1721.1/68485.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2011.
Vita. Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references.
Amyloid fibrils are insoluble, non-crystalline protein filaments associated with a number of diseases such as Alzheimer's and Type Il diabetes. They can have a functional role in different organisms and many proteins and peptides have been found to form amyloid fibrils in vitro. We have used magic angle spinning (MAS) NMR spectroscopy to investigate the structure of two amyloid fibril systems - an 11- residue segment from the disease-related protein transthyretin (TTR); and P2- microglobulin (32m), a 99-residue protein associated with dialysis-related amyloidosis. The TTR(105-115) case exemplifies our efforts to characterize the hierarchy of structures present in the fibril form, including the organization of the Pstrands into P-sheets (tertiary structure), the P-sheet interface that defines each protofilament (quaternary structure), and the protofilament-to-protofilament contacts that lead to the formation of the complete fibril. Our efforts were guided by information obtained from other methods such as cryo-electron microscopy and atomic force microscopy, and resulted in the very first atomic resolution structure of a complete amyloid fibril. We have extended the methods used in the TTR(105-115) structure determination procedure to the fibrils formed by 2m, a process complicated not only by the much larger size of the protein involved but also by the high degree of dynamics exhibited in these fibrils. Nevertheless, we were able to characterize the secondary structure of the protein in the fibril form, and the tertiary and quaternary interactions within the fibrils. In addition, we have compared at the molecular level @2m fibrils formed under different conditions, in an effort to characterize the origins of fibril polymorphism for this protein sequence. Our work on amyloid fibrils has also benefited extensively from the development of dynamic nuclear polarization, a method used to enhance the sensitivity of MAS NMR experiments, leading to unprecedented gains in signal-to-noise ratios and acquisition times.
by Galia Tzvetanova Debelouchina.
Ph.D.

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4

Unnikrishnan, Aparna. "INVESTIGATION OF PROTEIN STRUCTURE AND DYNAMICS BY NMR SPECTROSCOPY." The Ohio State University, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1595418229203869.

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Thurgood, Andrew G. P. "NMR studies of the structure and dynamics of proteins and peptides." Thesis, University of East Anglia, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253623.

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Rönnols, Jerk. "Structure, dynamics and reactivity of carbohydrates : NMR spectroscopic studies." Doctoral thesis, Stockholms universitet, Institutionen för organisk kemi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-92408.

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The main focus of this thesis is on the ring conformations of carbohydrate molecules; how the conformational equilibria and the rates of the associated interconversions are affected by the molecular constitution and their surroundings. The conformational equilibria of a group of amine linked pseudodisaccharides, designed as potential glycosidase inhibitors, comprising α-D-altrosides are described in Chapter 3. The OS2 conformation was largely populated, and the ring conformation was found to depend on the charge of the amine functionality. The conformations of β-D-xylopyranoside derivatives with naphthyl-based aglycones, which are potential anti-cancer agents, are described in chapter 4. Solvent dependent flexibility was observed. Intramolecular hydrogen bonds were concluded to be involved in the stabilization of 1C4 conformers in non-hydrogen bonding solvents of low polarity. Chapter 5 describes the first measurements of the conformational exchange rates of mannuronic acid ester derivatives between the 4C1 and 1C4 conformations, through DNMR measurements. The relative reactivity of glycosyl triflates as electrophiles in glycosylation reactions were investigated with NMR-based competition experiments. In Chapter 6, investigations of ruthenium-catalyzed epimerizations of the allylic alcohols of glycal derivatives, and stereoselective synthesis of esters through a DYKAT protocol, are described. The kinetics of the epimerizations were elaborated through different NMR-spectroscopic methods. Chapter 7 describes additions of NMR chemical shift data of mono- and oligosaccharides to database of the computer program CASPER, and applications thereof.

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 4: Submitted. Paper 5: Manuscript.

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Conroy, Daniel William. "Structural Studies of Biomolecules by Dynamic Nuclear Polarization Solid-State NMR Spectroscopy." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1555428362333615.

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8

Nagapudi, Karthik. "Solid-state NMR investigation of structure and dynamics of polyrotaxanes." Thesis, Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/8638.

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Tomaszewski, John William. "Structure and dynamics of small proteins by NMR /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/11541.

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10

Birk, Olsen Helle. "Investigations of structure and dynamics of insulin mutants using NMR spectroscopy /." Roskilde : Department of Life Sciences and Chemistry, Roskilde University, 1996. http://hdl.handle.net/1800/464.

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Books on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

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Berliner, Lawrence J., and N. Rama Krishna. Structure computation and dynamics in protein NMR. New York: Kluwer Academic, 2002.

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2

Rama, Krishna N., and Berliner Lawrence J, eds. Structure computation and dynamics in protein NMR. New York: Kluwer Academic/Plenum, 1999.

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3

Thurgood, Andrew G. P. NMR studies of the structure and dynamics of proteins and peptides. Norwich: University of East Anglia, 1990.

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4

Fedotov, V. D. Structure and dynamics of bulk polymers by NMR-methods. Berlin: Springer-Verlag, 1989.

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5

Berliner, Lawrence J., and N. Rama Krishna. Structure Computation and Dynamics in Protein NMR. Ingramcontent, 2013.

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6

Jackson, Michael B., and Vladimir D. Fedotov. Structure and Dynamics of Bulk Polymers by NMR-Methods. Springer, 2011.

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7

Philippopoulos, Marios. Comparative studies of protein structure and dynamics by molecular dynamics simulation, NMR spectroscopy and X-ray crystallography. 1999.

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8

Ollerenshaw, Jason Edward. Applications of liquid state NMR spectroscopy for protein structure, dynamics, and folding, and for quantum computation. 2005.

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Book chapters on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

1

Cross, T. A., F. Tian, M. Cotten, J. Wang, F. Kovacs, and R. Fu. "Correlations of Structure, Dynamics and Function in the Gramicidin Channel by Solid-State NMR Spectroscopy." In Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides, 4–22. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515716.ch2.

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2

Zhang, M., and H. J. Vogel. "Structure determination of the calmodulin binding domain of caldesmon by 2D NMR spectroscopy." In Peptides, 963–65. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_325.

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3

Kawamura, Izuru, Kazushi Norisada, and Akira Naito. "Structure Determination of Membrane Peptides and Proteins by Solid-State NMR." In Experimental Approaches of NMR Spectroscopy, 253–93. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-5966-7_9.

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Wray, Victor, Kiyoshi Nokihara, and Satoru Naruse. "Solution structure of PACAP by 1H NMR spectroscopy, distance geometry, and molecular dynamic calculations." In Peptide Chemistry 1992, 220–23. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1474-5_64.

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Tate, Shin-ichi. "Protein Structure and Dynamics Determination by Residual Anisotropic Spin Interactions." In Experimental Approaches of NMR Spectroscopy, 601–36. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-5966-7_22.

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Brown, Michael F. "Membrane Structure and Dynamics Studied with NMR Spectroscopy." In Biological Membranes, 175–252. Boston, MA: Birkhäuser Boston, 1996. http://dx.doi.org/10.1007/978-1-4684-8580-6_7.

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Koehl, Patrice, Bruno Kieffer, and Jean-François Lefèvre. "The Dynamics of Oligonucleotides and Peptides Determined by Proton NMR." In Protein Structure and Engineering, 139–54. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5745-2_10.

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Venkitakrishnan, Rani Parvathy, Outhiriaradjou Benard, Marianna Max, John L. Markley, and Fariba M. Assadi-Porter. "Use of NMR Saturation Transfer Difference Spectroscopy to Study Ligand Binding to Membrane Proteins." In Membrane Protein Structure and Dynamics, 47–63. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-023-6_4.

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Schmidt-Rohr, Klaus. "Dynamics and Structure of Amorphous Polymers Studied by Multidimensional Solid-State NMR Spectroscopy." In Multidimensional Spectroscopy of Polymers, 191–214. Washington, DC: American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0598.ch012.

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Vosegaard, Thomas, and Niels Chr Nielsen. "CHAPTER 14. NMR Investigations of the Structure and Dynamics of Antimicrobial Peptides: The Peptaibol Alamethicin." In New Developments in NMR, 267–86. Cambridge: Royal Society of Chemistry, 2014. http://dx.doi.org/10.1039/9781782627449-00267.

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Conference papers on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

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Miclet, Emeric, Anas Terrien, Claire Loison, Luminita Duma, Thierry Brigaud, Nathalie Lensen, Keyvan Rahgoshay, and Grégory Chaume. "New insights into the structural and dynamics properties of collagen model peptides using CD spectroscopy, MD simulations and innovative NMR approaches." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.192.

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Galanis, Athanassios S., Georgios A. Spyroulias, Roberta Pierattelli, Andreas Tzakos, Anastassios Troganis, George Pairas, Evi Manessi-Zoupa, Ioannis Gerothanassis, and Paul Cordopatis. "Structural studies through 1H NMR spectroscopy of somatic angiotensin converting enzyme (ACE) active sites and comparison with testis ACE crystal structure." In VIIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2003. http://dx.doi.org/10.1135/css200306029.

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Mukunoki, Atsushi, Tamotsu Chiba, Yasuhiro Suzuki, Kenji Yamaguchi, Tomofumi Sakuragi, and Tokuro Nanba. "Further Development of Iodine Immobilization Technique by Low Temperature Vitrification With BiPbO2I." In ASME 2009 12th International Conference on Environmental Remediation and Radioactive Waste Management. ASMEDC, 2009. http://dx.doi.org/10.1115/icem2009-16268.

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The authors describe progress in the development of low temperature vitrification with BiPbO2I (BPI) as a promising immobilization technique by which Iodine-129 is recovered by BiPbO2NO3 to form BPI, and then solidified into a lead-boron-zinc glass matrix (PbO-B2O3-ZnO) using a low temperature vitrification process. The microscopic structure of BPI glass was analyzed by various analytical techniques, such as XRD (X-ray diffraction), NMR (nuclear magnetic resonance analysis), and XPS (X-ray photoelectron spectroscopy), using several types of glass samples. The results obtained provide structural information on key elements in BPI glass and can be applied for modeling the structure of the BPI glass, simulated by molecular dynamics. The previous work suggested that the leaching behavior of iodine from BPI glass depended upon the chemical conditions of the solution. Further leaching tests using solutions under varying conditions were carried out in order to predict mechanisms of iodine leaching. Normalized elemental mass loss values of iodine in simulated seawater and bentonite pore water are almost the same as those of boron, showing that iodine dissolves congruently with BPI glass, whereas iodine dissolves incongruently in Ca(OH)2 solutions of pH 9 and 11. To demonstrate the feasibility of the BPI vitrification process, recovery tests of iodine from spent iodine filters were conducted and a prototype melting furnace was developed for scale-up tests of glass sample. It was found that more than 95% of iodine can be recovered from the spent iodine filter and that the prototype furnace can produce approximately 0.5 liters of homogeneous glass.

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Reports on the topic "Structure and Dynamics of Peptides by NMR Spectroscopy"

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Tiburu, Elvis K. Determination of the Dynamics, Structure, and Orientation of the Transmembrane Segment of ErbB2 in Model Membranes Using Solid-State NMR Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, March 2008. http://dx.doi.org/10.21236/ada482328.

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