Calcium-Binding Protein Protocols Calcium-Binding Protein Protocols

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Index 415 Terbium, see Fluorescence, terbium Thermodynamic parameters, 220, see also Calorimetry Thrombin, see Proteases, thrombin Tranilast, see Calmodulin, agonists Transfection, see Electroporation Transformation, see Bacterial transformation Troponin C, see also EF-hand proteins interaction with Troponin I, 153–155 U–W Ultraviolet spectroscopy, see Absorption spectroscopy UV-Vis Spectroscopy, see Absorption spectroscopy van’t Hoff enthalpy, see Enthalpy of protein unfolding Vanadyl, 201 Vector geometry mapping, 317–324 W7, see Calmodulin, agonists
METHODS IN MOLECULAR BIOLOGY TM • 173 Methods in Molecular BiologyTM • 173 CALCIUM-BINDING PROTEIN PROTOCOLS VOLUME II: METHODS AND TECHNIQUES ISBN: 0-89603-689-8 humanapress.com Series Editor: John M. Walker Calcium-Binding Protein Protocols Volume II: Methods and Techniques Edited by Hans J. Vogel Department of Biological Sciences, University of Calgary, Calgary, AB, Canada Calcium-binding proteins play an important role in a variety of vital biological processes, ranging from blood clotting and signal transduction in cells, to attaching proteins to membranes and serving as an integral source of calcium. In Calcium-Binding Protocols—Volume 1: Reviews and Case Studies and Volume 2: Methods and Techniques—Hans Vogel and a panel of leading researchers review the protein chemistry and behavior of this significant protein class, and provide a comprehensive collection of proven experimental techniques for their study both in vitro and in vivo. This second volume focuses on cutting-edge experimental techniques for studying the solution structure, stability, dynamics, calcium-binding properties, and biological activity of calcium-binding protein in general. In addition to enzymatic assays and more routine spectroscopic and protein chemistry techniques, there are also NMR approaches, thermodynamic analyses, kinetic measurements such as surface plasmon resonance, strategies for amino acid sequence alignments, and fluorescence methods to study the distribution of calcium and calcium-binding proteins in cells. The first companion volume, Reviews and Case Histories sets the stage for this volume by introducing the various classes of intra- and extracellular calcium-binding proteins and their mode of action. Comprehensive and highly practical, the two volumes of Calcium-Binding Protocols provide experimental and clinical biologists with a host of advanced experimental methods that can be applied successfully to the study of both existing and newly discovered members of this critically important class of proteins. • All major biophysical and protein methods to study calcium-binding proteins • Detailed discussion of calcium-binding proteins in vitro and in vivo Part III. Methods and Techniques to Study Calcium-Binding Proteins. Quantitative Analysis of Ca 2+ -Binding by Flow Dialysis. Calcium Binding to Proteins Studied via Competition with Chromophoric Chelators. Deconvolution of Calcium-Binding Curves: Facts and Fantasies. Absorption and Circular Dichroism Spectroscopy. Fourier Transform Infrared Spectroscopy of Calcium-Binding Proteins. Steady-State Fluorescence Spectroscopy. Fluorescence Methods for Measuring Calcium Affinity and Calcium Exchange with Proteins. Surface Plasmon Resonance of Calcium- Binding Proteins. Differential Scanning Calorimetry. Isothermal Titration Calorimetry. Multiangle Laser Light Scattering and Sedimentation Equilibrium. Small-Angle Solution Scattering Reveals Information on Conformational Dynamics in Calcium-Binding Proteins and in their Interactions with Regulatory Targets. Investigation of Calcium-Binding Proteins Using Electrospray Ionization Mass Spectrometry. Synthetic Calcium-Binding Peptides. Proteolytic Fragments of Calcium-Binding Proteins. Electron Magnetic Resonance Studies of Calcium-Binding Proteins. Cadmium-113 and Lead-207 NMR Spectroscopic Studies of Calcium-Binding Proteins. Calcium-43 of NMR of Calcium-Binding Proteins. Exploring Familial FEATURES CONTENTS • Methods using fluorescence spectroscopy, NMR, thermodynamic analysis, and kinetic measurements • Many methods also applicable to proteins that do not bind to calcium Relationships Using Multiple Sequence Alignment. Structure Determination by NMR: Isotope Labeling. Protein Structure Calculation from NMR Data. Shape and Dynamics of a Calcium-Binding Protein Investigated by Nitrogen-15 NMR Relaxation. The Use of Dipolar Couplings for the Structure Refinement of a Pair of Calcium-Binding EGF Domains. Vector Geometry Mapping: A Method to Characterize the Conformation of Helix- Loop-Helix Calcium-Binding Proteins. Use of Calmodulin Antagonists and S-100 Protein Interacting Drugs for Affinity Chromatography. Enzymatic Assays to Compare Calmodulin Isoforms, Mutants, and Chimeras. Gene Expression in Transfected Cells. Monitoring the Intracellular Free Ca 2+ -Calmodulin Concentration with Genetically-Encoded Fluorescent Indicator Proteins. Studying the Spatial Distribution of Ca 2+ -Binding Proteins: How Does it Work for Calmodulin? Index. 9 780896 036895 90000
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Methods in Molecular BiologyTM Biol
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M E T H O D S I N M O L E C U L A R
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© 2002 Humana Press Inc. 999 River
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Preface Calcium plays an important
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Contents Dedication ...............
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Contents xi 26 Enzymatic Assays to
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xiv Contents of Companion Volume 15
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xvi Contributors LESLIE D. HICKS
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20 Dean, Kelsey, and Re
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2 Yazawa
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4 Yazawa Fig. 1. Schematic represen
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6 Yazawa Fig. 2. Shop drawing for t
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8 Yazawa DuPont-NEN and the molar c
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10 Yazawa Fig. 4. Examples of the C
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12 Yazawa 5. Plot the calculated Ca
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14 Yazawa 12. Starovasnik, M. A., D
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16 Fig. 1. Molecular structures and
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18 Linse 7. 0.1 M EDTA. Dissolve 37
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20 Linse iterate the other paramete
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22 Linse tive to small alterations
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24 Linse References 1. Tsien, R. Y.
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26 Haiech and Kilhoffer to use the
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28 Haiech and Kilhoffer where γ is
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30 Haiech and Kilhoffer reporter gr
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32 Haiech and Kilhoffer tein with i
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34 Haiech and Kilhoffer Calmodulin
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36 Haiech and Kilhoffer Fig. 3. Mec
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38 Haiech and Kilhoffer We may sugg
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40 Haiech and Kilhoffer 29. Stewart
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42 Haiech and Kilhoffer 62. Becking
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44 Martin and Bayley Fig. 1. Absorp
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46 Martin and Bayley evaporation. C
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48 Martin and Bayley 4. Set the tem
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50 Martin and Bayley Fig. 2. Near-U
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52 Martin and Bayley discussed by M
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54 Martin and Bayley References 1.
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20 Dean, Kelsey, and Reik
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58 Fabian and Vogel are equipped wi
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60 Fabian and Vogel The penetration
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62 Fabian and Vogel perature, ionic
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64 Fabian and Vogel Fig. 3. IR spec
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66 Fabian and Vogel Fig. 4. Lower t
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68 Fabian and Vogel These correlati
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70 Fabian and Vogel Fig. 5. Amide I
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72 Fabian and Vogel 4. ATR-FTIR spe
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74 Fabian and Vogel 25. Georg, H.,
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76 Weljie and Vogel Fig. 1. Simplif
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78 Weljie and Vogel Fig. 3. Steady-
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80 Weljie and Vogel VIS spectrophot
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82 Weljie and Vogel 4. A series of
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84 Table 1 Advanced Fluorescence Me
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86 Weljie and Vogel References 1. L
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90 Johnson and Tikunova is removed
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92 Johnson and Tikunova function of
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94 Johnson and Tikunova Fig. 2. Rat
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96 Johnson and Tikunova Fig. 3. Rat
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98 Johnson and Tikunova Fig. 4. Ca
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100 Johnson and Tikunova cence inte
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102 Johnson and Tikunova 6. Johnson
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104 Julenius Fig. 1. Under conditio
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106 Julenius 3. Mix 50 µL of NHS s
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108 Julenius Fig. 3. A typical sens
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110 Julenius (2), is used in the Ia
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114 Lopez and Makhatadze Fig. 1. Th
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116 Lopez and Makhatadze 6. Buffers
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118 Lopez and Makhatadze The excess
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122 Lopez and Makhatadze Fig. 1. Is
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124 Lopez and Makhatadze 2.5 mL are
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126 Lopez and Makhatadze pendence o
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128 Hicks et al. equipped with a pu
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130 Hicks et al. Fig. 2. Debye plot
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132 Hicks et al. and 1.0 mg/mL for
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134 Hicks et al. Fig. 3. Sedimentat
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136 Hicks et al. 5. Hayes, D. B. (M
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138 Trewhella and Krueger This chap
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140 Trewhella and Krueger of the sc
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142 Trewhella and Krueger Table 1 C
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144 Trewhella and Krueger beam, or
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146 Trewhella and Krueger At very l
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148 Trewhella and Krueger analytica
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150 Trewhella and Krueger collapsed
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152 Trewhella and Krueger P(r) func
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154 Trewhella and Krueger Fig. 3. S
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156 Trewhella and Krueger concentra
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158 Trewhella and Krueger by a Nati
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162 Doherty-Kirby and Lajoie metal
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164 Doherty-Kirby and Lajoie two Ca
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166 Doherty-Kirby and Lajoie 7. Pep
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168 Doherty-Kirby and Lajoie Fig. 1
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170 Doherty-Kirby and Lajoie Fig. 2
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172 Doherty-Kirby and Lajoie 5. Alt
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174 Doherty-Kirby and Lajoie phosph
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176 Shaw Fig. 1. Ribbon drawing of
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178 Shaw 2.3. Other 1. Chemicals fo
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180 Shaw 3.3.3. Purification 1. Con
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182 Shaw 10. Hodges, R. S., Semchuk
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184 Brokx and Vogel Table 1 An Over
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186 Brokx and Vogel Fig. 1. UV abso
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188 Brokx and Vogel Fig. 2. 20% SDS
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190 Brokx and Vogel it through an a
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192 Brokx and Vogel 8. Weljie, A. M
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196 Berliner Fig. 1. Aqueous X-band
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198 Berliner in the Bruker instrume
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200 Berliner Fig. 3. ESR spectra of
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202 Berliner Fig. 5. Low-temperatur
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204 Berliner 14. Musci, G., Reed, G
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206 Clarke and Vogel cal calcium-bi
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208 Clarke and Vogel Fig. 1. 113 Cd
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214 Clarke and Vogel The linewidth
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218 Drakenberg sands, of Hertz broa
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220 Drakenberg 1. Bloch equations m
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222 Drakenberg Fig. 2. Measurement
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224 Drakenberg Fig. 3. (A) 43 Ca NM
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226 Drakenberg Fig. 5. 43 Ca NMR sp
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228 Drakenberg NMR at sub-mM concen
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230 Drakenberg 30. Shimizu, T., Hat
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232 Weljie and Heringa Table 1 Amin
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234 Weljie and Heringa Table 2 Webs
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236 Weljie and Heringa diction meth
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238 Weljie and Heringa these databa
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240 Weljie and Heringa lineages. Th
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242 Weljie and Heringa compared, an
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244 Weljie and Heringa sequences as
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246 Weljie and Heringa much larger
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248 Weljie and Heringa ment require
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250 Weljie and Heringa 10. Kawasaki
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252 Weljie and Heringa 44. Thompson
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254 Weljie and Heringa
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256 Li et al. In order for these ex
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258 Li et al. 7. Mineral Mixture (s
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260 Li et al. 3. When the 45% D 2O/
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262 Li et al. sion system works eff
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264 Li et al. reliably produce high
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268 Mal et al. NMR data, X-PLOR (11
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270 Mal et al. Table 1 Simulated An
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272 Mal et al. 3.1.2.1. AMBIGUOUS D
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274 Mal et al. molecular dynamics a
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276 Mal et al. Assuming a rigid bod
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278 Mal et al. assign (segid A and
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280 Mal et al. References 1. Drenth
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282 Mal et al. 33. Jeener, J., Meie
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286 Werner et al. Our research has
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288 Fig. 1. (A) T 1, T 2 and the he
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290 Werner et al. tion, using gradi
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292 Werner et al. Fig. 3. (A) Rotat
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294 Werner et al. Fig. 4. (A) Line-
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296 Werner et al. Table 2 Models of
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298 Werner et al. 9. Reinhardt, D.
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300 Werner et al. 39. Press, W. H.,
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302 Boyd et al. utilize residual di
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304 Boyd et al. Fig. 1. (A) The sol
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306 Boyd et al. or significant peak
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308 Boyd et al. Fig. 3. Histogram o
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310 Boyd et al. total and NOE energ
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312 Boyd et al. 2. When studying mu
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314 Boyd et al. 4. Downing, A. K.,
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316 Boyd et al. 35. Schulte-Herbrug
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318 Yap et al. image representation
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320 Yap et al. modified EF-hand is
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322 Table 1 Angle and Distance Outp
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324 Yap et al. 2. Ikura, M. (1995)
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326 Kobayashi that S-100A1 and S-10
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328 Kobayashi 3.2. Coupling of Crom
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330 Kobayashi Fig. 2. Tricine/SDS/P
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332 Kobayashi 0.1% TFA at a flow ra
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334 Kobayashi Both recombinant S-10
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336 Kobayashi Fig. 6. Affinity chro
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340 Walsh et al. verts CaM from an
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342 Walsh et al. 11. Bovine serum a
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344 Walsh et al. Fig. 1. CaM-depend
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348 Walsh et al. 3.5. NOS Reduction
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354 Walsh et al. 3. Cho, M. J., Vag
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356 Hughes et al. The electroporati
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358 Hughes et al. 4. 1 M Na 2CO 3.
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360 Hughes et al. range, repeat ste
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362 Hughes et al. Table 1 Examples
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Page 385 and 386: 366 Persechini of the different CaM
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Page 429 and 430: 410 Index substitutes, see Fluoresc
Page 431 and 432: 412 Index Stern-Volmer plot, 78, 81
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