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Pressure jump

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Historically, pressure jumps were limited to one direction. Most commonly fast drops in pressure were achieved by using a quick release valve or a fast burst membrane. Modern equipment can achieve pressure changes in both directions using either double reservoir arrangements (good for large changes
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Malnási-Csizmadia, A; Pearson, D.S.; Kovács, M.; Woolley, R.J.; Geeves, M.A.; Bagshaw, C.R. (2001). "Kinetic Resolution of a Conformational Transition and the ATP Hydrolysis Step Using Relaxation Methods with a Dictyostelium Myosin II Mutant Containing a Single Tryptophan Residue".
59:(often faster than valve based approaches). Ultra fast pressure drops can be achieved using electrically disintegrated burst membranes. The ability to automatically repeat measurements and average the results is useful since the reaction amplitudes are often small. 162: 423:"A novel pressure jump apparatus for the microvolume analysis of protein-ligand and protein-protein interactions: its application to nucleotide binding to skeletal-muscle and smooth-muscle myosin subfragment 1" 198:(1/Ď„) equal to the sum of the forward and reverse intrinsic rate constants. In more complex reaction networks, when multiple reaction steps are perturbed, then the reciprocal time constants are given by the 31:. This allows the study of the shift in equilibrium of reactions that equilibrate in periods between milliseconds to hours (or longer), these changes often being observed using 202:
of the characteristic rate equations. The ability to observe intermediate steps in a reaction pathway is one of the attractive features of this technology.
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Heuer U, Krumova M, Hempel G, Schiewek M, Blume A (2010). "NMR probe for pressure-jump experiments up to 250 bars and 3 ms jump time".
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Schiewek M, Krumova M, Hempel G, Blume A (2007). "Pressure jump relaxation setup with IR detection and millisecond time resolution".
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Marchal S, Font J, RibĂł M, Vilanova M, Phillips RS, Lange R, Torrent J (2009). "Asymmetric kinetics of protein structural changes".
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Dumont C, Emilsson T, Gruebele M (2009). "Reaching the protein folding speed limit with large, sub-microsecond pressure jumps".
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Methods for studying fast kinetics in biological systems in: Davies DB, Saenger W, Danyluk SS (Eds) Structural Molecular Biology
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Gruenewald B, Knoche W (1978). "Pressure jump method with detection of optical-rotation and circular-dichroism".
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When a single step in a reaction is perturbed in a pressure jump experiment, the reaction follows a single
23:. It involves making rapid changes to the pressure of an experimental system and observing the return to 547: 48: 180: 66:
the percentage change in concentration of a measurable species) depends on the molar volume change (Δ
36: 28: 32: 56: 327: 284: 241: 183:. The volume change can thus be understood to be the pressure dependency of the change in 24: 8: 331: 288: 245: 447: 422: 40: 523: 487: 452: 403: 366: 343: 300: 257: 191: 184: 157:{\displaystyle \Delta V^{o}=-RT\left({\frac {\partial \ln K}{\partial P}}\right)_{T}} 20: 515: 479: 442: 434: 395: 335: 292: 249: 219: 541: 195: 527: 491: 456: 407: 347: 304: 261: 172: 222:
in which cooling curves typically limit the time window to a minute or so.
70:°) between the reactants and products and the equilibrium position. If 483: 438: 199: 519: 399: 339: 296: 253: 504: 421:
Pearson DS, Holtermann G, Ellison P, Cremo C, Geeves MA (2002).
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is the pressure then the volume change is given by:
156: 539: 498: 231: 39:though other spectroscopic techniques such as 360: 446: 225: 268: 62:The fractional extent of the reaction ( 540: 414: 379: 463: 311: 55:in pressure) or pistons operated by 19:is a technique used in the study of 13: 135: 121: 88: 14: 559: 320:Review of Scientific Instruments 277:Review of Scientific Instruments 234:Review of Scientific Instruments 74:is the equilibrium constant and 354: 212: 187:associated with the reaction. 1: 388:Accounts of Chemical Research 205: 194:function with the reciprocal 7: 10: 564: 365:. Plenum Publishing Corp. 37:fluorescence spectroscopy 57:piezoelectric actuators 33:absorption spectroscopy 173:universal gas constant 158: 159: 218:This contrasts with 181:absolute temperature 85: 427:Biochemical Journal 361:Pörschke D (1982). 332:2010RScI...81j5102H 289:2007RScI...78d5101S 246:1978RScI...49..797G 484:10.1038/nmeth.1336 439:10.1042/BJ20020462 154: 51:can also be used. 548:Chemical kinetics 520:10.1021/bi010963q 400:10.1021/ar800266r 340:10.1063/1.3481164 297:10.1063/1.2719020 254:10.1063/1.1135618 192:exponential decay 185:Gibbs free energy 142: 21:chemical kinetics 555: 532: 531: 502: 496: 495: 467: 461: 460: 450: 418: 412: 411: 383: 377: 376: 358: 352: 351: 315: 309: 308: 272: 266: 265: 229: 223: 220:temperature jump 216: 163: 161: 160: 155: 153: 152: 147: 143: 141: 133: 119: 100: 99: 563: 562: 558: 557: 556: 554: 553: 552: 538: 537: 536: 535: 514:: 12727–12737. 503: 499: 468: 464: 419: 415: 384: 380: 373: 359: 355: 316: 312: 273: 269: 230: 226: 217: 213: 208: 148: 134: 120: 118: 114: 113: 95: 91: 86: 83: 82: 12: 11: 5: 561: 551: 550: 534: 533: 497: 472:Nature Methods 462: 413: 378: 371: 353: 310: 267: 224: 210: 209: 207: 204: 165: 164: 151: 146: 140: 137: 132: 129: 126: 123: 117: 112: 109: 106: 103: 98: 94: 90: 9: 6: 4: 3: 2: 560: 549: 546: 545: 543: 529: 525: 521: 517: 513: 509: 501: 493: 489: 485: 481: 477: 473: 466: 458: 454: 449: 444: 440: 436: 432: 428: 424: 417: 409: 405: 401: 397: 393: 389: 382: 374: 372:0-306-40982-8 368: 364: 357: 349: 345: 341: 337: 333: 329: 325: 321: 314: 306: 302: 298: 294: 290: 286: 282: 278: 271: 263: 259: 255: 251: 247: 243: 239: 235: 228: 221: 215: 211: 203: 201: 197: 196:time constant 193: 188: 186: 182: 178: 174: 170: 149: 144: 138: 130: 127: 124: 115: 110: 107: 104: 101: 96: 92: 81: 80: 79: 77: 73: 69: 65: 60: 58: 52: 50: 46: 42: 38: 34: 30: 26: 22: 18: 17:Pressure jump 511: 508:Biochemistry 507: 500: 478:(7): 515–9. 475: 471: 465: 430: 426: 416: 391: 387: 381: 362: 356: 323: 319: 313: 280: 276: 270: 237: 233: 227: 214: 189: 176: 168: 166: 75: 71: 67: 63: 61: 53: 29:steady state 16: 15: 433:: 643–651. 240:: 797–801. 200:eigenvalues 25:equilibrium 394:: 778–87. 326:: 105102. 283:: 045101. 206:References 136:∂ 128:⁡ 122:∂ 105:− 89:Δ 542:Category 528:11601998 492:19483692 457:12010120 408:19378977 348:21034114 305:17477687 262:18699196 448:1222786 328:Bibcode 285:Bibcode 242:Bibcode 179:is the 171:is the 526:  490:  455:  445:  406:  369:  346:  303:  260:  167:where 35:, or 524:PMID 488:PMID 453:PMID 404:PMID 367:ISBN 344:PMID 301:PMID 258:PMID 175:and 64:i.e. 45:FTIR 516:doi 480:doi 443:PMC 435:doi 431:366 396:doi 336:doi 293:doi 250:doi 49:NMR 47:or 27:or 544:: 522:. 512:40 510:. 486:. 474:. 451:. 441:. 429:. 425:. 402:. 392:42 390:. 342:. 334:. 324:81 322:. 299:. 291:. 281:78 279:. 256:. 248:. 238:49 236:. 125:ln 43:, 41:CD 530:. 518:: 494:. 482:: 476:6 459:. 437:: 410:. 398:: 375:. 350:. 338:: 330:: 307:. 295:: 287:: 264:. 252:: 244:: 177:T 169:R 150:T 145:) 139:P 131:K 116:( 111:T 108:R 102:= 97:o 93:V 76:P 72:K 68:V

Index

chemical kinetics
equilibrium
steady state
absorption spectroscopy
fluorescence spectroscopy
CD
FTIR
NMR
piezoelectric actuators
universal gas constant
absolute temperature
Gibbs free energy
exponential decay
time constant
eigenvalues
temperature jump
Bibcode
1978RScI...49..797G
doi
10.1063/1.1135618
PMID
18699196
Bibcode
2007RScI...78d5101S
doi
10.1063/1.2719020
PMID
17477687
Bibcode
2010RScI...81j5102H

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