Calcium-Binding Protein Protocols Calcium-Binding Protein Protocols

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Electron Magnetic Resonance Studies 203 domain. By adding saturated sucrose to the sample, the splittings in the EPR spectra will move outward (i.e., increase), frequently revealing other motional components that might exist (3). Another technique involves increasing the modulation and receiver gain four- to fivefold, consequently overmodulating the narrow line components and emphasizing the broad slow motional components. Acknowledgment This work was supported in part by grants from the U.S.P.H.S. References 1. Berliner, L. J., ed. (1976) Spin Labeling: Theory and Applications. Academic, New York, New York. 2. Berliner, L. J., ed. (1979) Spin Labeling II: Theory and Applications. Academic, New York, New York. 3. Berliner, L. J. (1980) Using the spin label method in enzymology, in Spectroscopy in Biochemistry, vol. II, CRC, West Palm Beach, Florida, pp. 1–56 . 4. Berliner, L. J. (1983) The spin labeling approach to labeling sulfhydryl groups in membrane proteins. Ann. NY Acad. Sci. 414 153–161. 5. Eaton, G. R., Eaton, S. S., and Berliner, L. J., eds. (2000) Distance measurements in biological systems by EPR, in Biological Magnetic Resonance, vol. 19, Kluwer Academic/Plenum, New York. 6. Musci, G., Koga, K., and Berliner, L. J. (1988) Met-90 spin-labeled bovine α-lactalbumin: ESR and NMR distance measurements. Biochemistry 27, 1260–1265. 7. Berliner, L. J. (1977) Spin labeling in enzymology — spin labeled enzymes and proteins. Methods Enzymol. 49G, 418–480. 8. Koga, K. and Berliner, L. J. (1985) Structural elucidation of a hydrophobic box in bovine a-lactalbumin by NMR: nuclear Overhauser effects. Biochemistry 24, 7257–7262. 9. Feix, J. B. and Klug, C. S. (1998) Site-directed spin labeling of membrane proteins and peptide-membrane interactions, in Spin Labeling: The Next Millennium, Biological Magnetic Resonance, vol. 14 (Berliner, L. J., ed.), Plenum, New York, pp. 251–281. 10. Jost, P. C. and Griffith, O. H. (1976) Instrumental aspects or spin labeling, in Spin Labeling: Theory and Applications (Berliner, L. J., ed.), Academic, New York. 11. Berliner, L. J., Ellis, P. D., and Murakami, K. (1983) Mn(II) and 113-Cd NMR evidence for the nature of the Ca(II) binding site in α-lactalbumin. Biochemistry 22, 5061–5063. 12. Buttlaire, D. H., Reed, G. H., and Himes, R. (1975) Electron paramagnetic resonance and water proton relaxation rate studies of formyltetrahydrofolate synthetasemanganous ion complexes. Evidence for involvement of substrates in the promotion of a catalytically competent active site. J. Biol. Chem. 250, 261–270. 13. Reed, G. H. and Markham, G. D. (1984) EPR of Mn(II) complexes with and enzymes other proteins, in Biological Magnetic Resonance, vol. 6 (Berliner, L. J., ed.), Plenum, New York, pp. 73–142.
204 Berliner 14. Musci, G., Reed, G. H., and Berliner, L. J. (1986) An electron paramagnetic resonance study of metal ion binding to bovine α-lactalbumin. J. Inorg. Biochem. 26, 229–236. 15. Chasteen, N. D. (1995) Vanadium-protein interactions. Metal Ions Biol. Syst. 31, 231–247. 16. Acharya, K. R., Ren, J., Stuart, D. I., and Phillips, D. C. (1991) Crystal structure of human α-lactalbumin at 1. 7 Å resolution. J. Mol. Biol. 221, 571–581.
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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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Page 227 and 228: 208 Clarke and Vogel Fig. 1. 113 Cd
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Page 237 and 238: 218 Drakenberg sands, of Hertz broa
Page 239 and 240: 220 Drakenberg 1. Bloch equations m
Page 241 and 242: 222 Drakenberg Fig. 2. Measurement
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Page 265 and 266: 246 Weljie and Heringa much larger
Page 267 and 268: 248 Weljie and Heringa ment require
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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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366 Persechini of the different CaM
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368 Persechini Fig. 1. Schematic re
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370 Persechini 2. 1 L of Terrific b
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372 Persechini Fig. 4. Titration wi
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374 Persechini Table 1 Parameters f
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376 Persechini Fig. 6. The [Ca 2+ -
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378 Persechini determined if the di
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380 Persechini relatively insensiti
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382 Persechini 18. Chafouleas, J. G
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384 Török et al. actions in the c
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386 Török et al. 3. The reaction
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388 Török et al. Fig. 2. Electros
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390 Török et al. Fig. 3. Peptides
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392 Török et al. Table 1 Peptide
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394 Török et al. Fig. 7. Nanospra
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396 Török et al. Fig. 9. Nanospra
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398 Török et al. Fig. 11. Electro
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400 Török et al. 3 µM FL-calmodu
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402 Török et al. Fig. 14. Localiz
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404 Török et al. Fig. 16. Indicat
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406 Török et al. the significantl
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408 Török et al.
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410 Index substitutes, see Fluoresc
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412 Index Stern-Volmer plot, 78, 81
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414 Index Phenothiazines, see Calmo
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