Skip to main content
SpringerLink
Log in

Biochemical effects of molecular crowding

  • Review
  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

Cell cytoplasm contains high concentrations of high-molecular-weight components that occupy a substantial part of the volume of the medium (crowding conditions). The effect of crowding on biochemical processes proceeding in the cell (conformational transitions of biomacromolecules, assembling of macromolecular structures, protein folding, protein aggregation, etc.) is discussed in this review. The excluded volume concept, which allows the effects of crowding on biochemical reactions to be quantitatively described, is considered. Experimental data demonstrating the biochemical effects of crowding imitated by both low-molecular-weight and high-molecular-weight crowding agents are summarized.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

GAPD:

D-glyceraldehyde 3-phosphate dehydrogenase

PDI:

protein disulfide isomerase

PEG:

polyethylene glycol

TMAO:

trimethylamine N-oxide

HbCN:

cyanomethemoglobin

REFERENCES

  1. A. B. Fulton (1982) Cell 30 345–347 Occurrence Handle6754085 Occurrence Handle1:STN:280:DyaL3s%2FltV2iuw%3D%3D

    PubMed  CAS  Google Scholar 

  2. S. B. Zimmerman S. O. Trach (1991) J. Mol. Biol. 222 599–620 Occurrence Handle1748995 Occurrence Handle1:CAS:528:DyaK38XlsFanuw%3D%3D

    PubMed  CAS  Google Scholar 

  3. R. J. Ellis A. P. Minton (2003) Nature 425 27–28 Occurrence Handle12955122 Occurrence Handle1:CAS:528:DC%2BD3sXmvFaguro%3D

    PubMed  CAS  Google Scholar 

  4. O. Medalia I. Weber A. S. Frangakis D. Nicastro G. Gerisch W. Baumeister (2002) Science 298 1209–1213 Occurrence Handle12424373 Occurrence Handle1:CAS:528:DC%2BD38XosVertbY%3D

    PubMed  CAS  Google Scholar 

  5. S. B. Zimmerman A. P. Minton (1993) Annu. Rev. Biophys. Biomol. Struct. 22 27–65 Occurrence Handle7688609 Occurrence Handle1:CAS:528:DyaK3sXlsFCjurg%3D

    PubMed  CAS  Google Scholar 

  6. A. P. Minton (2001) J. Biol. Chem. 276 10577–10580 Occurrence Handle11279227 Occurrence Handle1:CAS:528:DC%2BD3MXjvFCqtr8%3D

    PubMed  CAS  Google Scholar 

  7. R. J. Ellis (2001) Trends Biochem. Sci. 26 597–604 Occurrence Handle11590012 Occurrence Handle1:CAS:528:DC%2BD3MXnt1Wjsbc%3D

    PubMed  CAS  Google Scholar 

  8. K. Grunewald O. Medalia A. Gross A. Steven W. Baumeister (2003) Biophys. Chem. 100 577–591 Occurrence Handle12646392 Occurrence Handle1:CAS:528:DC%2BD3sXitFalsr0%3D

    PubMed  CAS  Google Scholar 

  9. A. Verkman (2002) Trends Biochem. Sci. 27 27–33 Occurrence Handle11796221 Occurrence Handle1:CAS:528:DC%2BD38XktVOmtA%3D%3D

    PubMed  CAS  Google Scholar 

  10. A. E. Lyubarev B. I. Kurganov (1996) NoChapterTitle B. I. Kurganov A. E. Lyubarev (Eds) Organization of Biochemical Systems: Structural and Regulatory Aspects Nova Science N. Y. 1–81

    Google Scholar 

  11. D. Hall A. P. Minton (2003) Biochim. Biophys. Acta 1649 127–139 Occurrence Handle12878031 Occurrence Handle1:CAS:528:DC%2BD3sXls1CjsbY%3D

    PubMed  CAS  Google Scholar 

  12. A. P. Minton (1981) Biopolymers 20 2093–2120 Occurrence Handle1:CAS:528:DyaL3MXlvVaktb8%3D

    CAS  Google Scholar 

  13. A. P. Minton (1983) Mol. Cell. Biochem. 55 119–140 Occurrence Handle6633513 Occurrence Handle1:CAS:528:DyaL3sXlvFSjsbg%3D

    PubMed  CAS  Google Scholar 

  14. P. R. Wills D. J. Winzor (1993) Biopolymers 33 1627–1629 Occurrence Handle1:CAS:528:DyaK2cXjtVag

    CAS  Google Scholar 

  15. P. R. Wills W. D. Comper D. J. Winzor (1993) Arch. Biochem. Biophys. 300 206–212 Occurrence Handle8424654 Occurrence Handle1:CAS:528:DyaK3sXhtFSkurc%3D

    PubMed  CAS  Google Scholar 

  16. C. L. Winzor D. J. Winzor L. G. Paleg G. P. Jones B. P. Naidu (1992) Arch. Biochem. Biophys. 296 102–107 Occurrence Handle1605623 Occurrence Handle1:CAS:528:DyaK38XksVegtL8%3D

    PubMed  CAS  Google Scholar 

  17. D. J. Winzor P. R. Wills (1995) NoChapterTitle R. B. Gregory (Eds) Protein—Solvent Interactions Marcel Dekker N. Y. 483–520

    Google Scholar 

  18. D. J. Winzor P. R. Wills (1995) Biophys. Chem. 57 103–110 Occurrence Handle8534833 Occurrence Handle1:CAS:528:DyaK2MXos1Ggs7w%3D

    PubMed  CAS  Google Scholar 

  19. P. R. Davis-Searles A. J. Saunders D. A. Erie D. J. Winzor G. J. Pielak (2001) Annu. Rev. Biophys. Biomol. Struct. 30 271–306 Occurrence Handle11340061 Occurrence Handle1:CAS:528:DC%2BD3MXkvVaqtr4%3D

    PubMed  CAS  Google Scholar 

  20. A. P. Minton (2001) Biophys. J. 80 1641–1648 Occurrence Handle11259279 Occurrence Handle1:CAS:528:DC%2BD3MXkvFWjurw%3D

    PubMed  CAS  Google Scholar 

  21. T. C. Laurent (1963) Biochem. J. 89 253–257 Occurrence Handle14084609 Occurrence Handle1:CAS:528:DyaF2cXjt1Wnuw%3D%3D

    PubMed  CAS  Google Scholar 

  22. P. D. Ross A. P. Minton (1977) J. Mol. Biol. 112 437–452 Occurrence Handle875025 Occurrence Handle1:CAS:528:DyaE2sXksl2qtr0%3D

    PubMed  CAS  Google Scholar 

  23. A. P. Minton J. Wilf (1981) Biochemistry 20 4821–4826 Occurrence Handle7295652 Occurrence Handle1:CAS:528:DyaL3MXkvFaqtbo%3D

    PubMed  CAS  Google Scholar 

  24. J. Monod J. Wyman J. P. Changeux (1965) J. Mol. Biol. 12 88–118 Occurrence Handle14343300 Occurrence Handle1:CAS:528:DyaF2MXkt1Ghsb4%3D Occurrence Handle10.1016/S0022-2836(65)80285-6

    Article  PubMed  CAS  Google Scholar 

  25. A. P. Minton (1990) Int. J. Biochem. 22 1063–1067 Occurrence Handle2289612 Occurrence Handle1:CAS:528:DyaK3MXjslygsA%3D%3D

    PubMed  CAS  Google Scholar 

  26. G. B. Ralston (1990) J. Chem. Educ. 67 857–860 Occurrence Handle1:CAS:528:DyaK3MXlsVGj Occurrence Handle10.1021/ed067p857

    Article  CAS  Google Scholar 

  27. D. Hall A. P. Minton (2004) Biophys. Chem. 107 299–316 Occurrence Handle14967245 Occurrence Handle1:CAS:528:DC%2BD2cXht1Klsr0%3D

    PubMed  CAS  Google Scholar 

  28. B. Farruggia B. Nerli G. Pico (2003) J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 798 25–33 Occurrence Handle14630355 Occurrence Handle1:CAS:528:DC%2BD3sXptVegu74%3D

    PubMed  CAS  Google Scholar 

  29. B. Farruggia G. Garcia C. D’Angelo G. Pico (1997) Int. J. Biol. Macromol. 20 43–51 Occurrence Handle9110184 Occurrence Handle1:CAS:528:DyaK2sXislOntLo%3D

    PubMed  CAS  Google Scholar 

  30. N. Tokuriki M. Kinjo S. Negi M. Hoshino Y. Goto I. Urabe T. Yomo (2004) Prot. Sci. 13 125–133 Occurrence Handle1:CAS:528:DC%2BD2cXhsFWisA%3D%3D

    CAS  Google Scholar 

  31. K. Sasahara P. McPhie A. P. Minton (2003) J. Mol. Biol. 326 1227–1237 Occurrence Handle12589765 Occurrence Handle1:CAS:528:DC%2BD3sXhtVCiurg%3D

    PubMed  CAS  Google Scholar 

  32. K. W. Minton P. Karmin G. M. Hahn A. P. Minton (1982) Proc. Natl. Acad. Sci. USA 79 7107–7111 Occurrence Handle6961397 Occurrence Handle1:CAS:528:DyaL3sXivF2ntQ%3D%3D

    PubMed  CAS  Google Scholar 

  33. G. Rivas J. A. Fernandez A. P. Minton (1999) Biochemistry 38 9379–9388 Occurrence Handle10413513 Occurrence Handle1:CAS:528:DyaK1MXktFSlsLg%3D

    PubMed  CAS  Google Scholar 

  34. G. Rivas J. A. Fernandez A. P. Minton (2001) Proc. Natl. Acad. Sci. USA 98 3150–3155 Occurrence Handle11248047 Occurrence Handle1:CAS:528:DC%2BD3MXit1als7w%3D

    PubMed  CAS  Google Scholar 

  35. J. Wilf A. P. Minton (1981) Biochim. Biophys. Acta 670 316–322 Occurrence Handle6271244 Occurrence Handle1:CAS:528:DyaL38XmsVertg%3D%3D

    PubMed  CAS  Google Scholar 

  36. J. Torbert (1986) Biochemistry 25 5309–5314

    Google Scholar 

  37. D. Drenckhahn T. D. Pollard (1986) J. Biol. Chem. 261 12754–12758 Occurrence Handle3745211 Occurrence Handle1:CAS:528:DyaL28XlvVKiurs%3D

    PubMed  CAS  Google Scholar 

  38. R. L. Tellam M. J. Sculley L. W. Nichol (1983) Biochem. J. 213 651–659 Occurrence Handle6412688 Occurrence Handle1:CAS:528:DyaL3sXltFyju7g%3D

    PubMed  CAS  Google Scholar 

  39. H. J. Bosma G. Voordouw A. Kok Particlede C. Veeger (1980) FEBS Lett. 120 179–182 Occurrence Handle7439395 Occurrence Handle1:CAS:528:DyaL3MXhsFKj

    PubMed  CAS  Google Scholar 

  40. S. B. Zimmerman S. O. Trach (1988) Nucleic Acids Res. 16 6309–6326 Occurrence Handle3041372 Occurrence Handle1:CAS:528:DyaL1cXlsVCktr4%3D

    PubMed  CAS  Google Scholar 

  41. T. C. Jarvis D. M. Ring S. S. Daube P. H. Hippel Particlevon (1990) J. Biol. Chem. 265 15160–15167 Occurrence Handle2168402 Occurrence Handle1:CAS:528:DyaK3cXlvVKks7Y%3D

    PubMed  CAS  Google Scholar 

  42. B. I. Kurganov I. N. Topchieva N. P. Lisovskaya N. A. Chebotareva O. Y. Natarius (1979) Biokhimiya 44 629–633 Occurrence Handle1:CAS:528:DyaE1MXktFGqsL4%3D

    CAS  Google Scholar 

  43. G. Ren Z. Lin C. L. Tsou C. C. Wang (2003) J. Prot. Chem. 22 431–439 Occurrence Handle1:CAS:528:DC%2BD3sXptlGluro%3D

    CAS  Google Scholar 

  44. H. R. Sunshine J. Hofrichter W. A. Eaton (1979) J. Mol. Biol. 133 435–467 Occurrence Handle94101 Occurrence Handle1:CAS:528:DyaL3cXhslCksA%3D%3D

    PubMed  CAS  Google Scholar 

  45. V. Uversky M. Cooper K. Bower J. Li A. Fink (2001) FEBS Lett. 515 99–103

    Google Scholar 

  46. M. D. Shtilerman T. T. Ding P. T. Lansbury SuffixJr. (2002) Biochemistry 41 3855–3860 Occurrence Handle11900526 Occurrence Handle1:CAS:528:DC%2BD38XhsV2hsL8%3D

    PubMed  CAS  Google Scholar 

  47. D. M. Hatters A. P. Minton G. J. Howlett (2002) J. Biol. Chem. 277 7824–7830 Occurrence Handle11751863 Occurrence Handle1:CAS:528:DC%2BD38XitFynu7s%3D

    PubMed  CAS  Google Scholar 

  48. N. Kozer G. Schreiber (2004) J. Mol. Biol. 336 763–774 Occurrence Handle15095986 Occurrence Handle1:CAS:528:DC%2BD2cXptFSntQ%3D%3D

    PubMed  CAS  Google Scholar 

  49. S. E. Harding A. J. Rowe J. C. Horton (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science Royal Society of Chemistry Cambridge

    Google Scholar 

  50. G. Rivas A. P. Minton (2003) Biochem. Soc. Trans. 31 1015–1019 Occurrence Handle14505471 Occurrence Handle1:CAS:528:DC%2BD3sXnsVyjt7g%3D

    PubMed  CAS  Google Scholar 

  51. D. K. Eggers J. V. Valentine (2001) J. Mol. Biol. 314 911–922 Occurrence Handle11734007 Occurrence Handle1:CAS:528:DC%2BD3MXosl2ju7Y%3D

    PubMed  CAS  Google Scholar 

  52. D. L. D. Caspar A. Klug (1962) Cold Spring Harbor Symp. 27 1–24 Occurrence Handle1:STN:280:DyaF383htFSnug%3D%3D

    CAS  Google Scholar 

  53. C. B. Anfinsen (1973) Science 181 223–230 Occurrence Handle4124164 Occurrence Handle1:CAS:528:DyaE3sXkvVygtbc%3D

    PubMed  CAS  Google Scholar 

  54. R. J. Ellis (1987) Nature 328 378–379 Occurrence Handle10.1038/328378a0 Occurrence Handle1:STN:280:DyaL2s3oslWqtQ%3D%3D Occurrence Handle3112578

    Article  CAS  PubMed  Google Scholar 

  55. R. J. Ellis S. M. Hemmingsen (1989) Trends Biochem. Sci. 14 339–342 Occurrence Handle2572080 Occurrence Handle1:CAS:528:DyaL1MXlvV2ltrk%3D

    PubMed  CAS  Google Scholar 

  56. F. U. Hartl M. Hayer-Hartl (2002) Science 295 1852–1858 Occurrence Handle10.1126/science.1068408 Occurrence Handle1:CAS:528:DC%2BD38XhvFClsL4%3D Occurrence Handle11884745

    Article  CAS  PubMed  Google Scholar 

  57. K. A. Markossian B. I. Kurganov (2004) Biochemistry (Moscow) 69 971–984 Occurrence Handle1:CAS:528:DC%2BD2cXotVGnuro%3D

    CAS  Google Scholar 

  58. V. R. Agashe F.-U. Hartle (2000) Semin. Cell Dev. Biol. 11 15–25 Occurrence Handle10736260 Occurrence Handle1:CAS:528:DC%2BD3cXivF2murY%3D

    PubMed  CAS  Google Scholar 

  59. P. B. Sigler Z. Xu H. S. Rye S. G. Burston W. A. Fenton A. L. Horwich (1998) Annu. Rev. Biochem. 67 581–608 Occurrence Handle9759498 Occurrence Handle1:CAS:528:DyaK1cXlsFOmsb0%3D

    PubMed  CAS  Google Scholar 

  60. M. E. Gottesman W. A. Hendrickson (2000) Curr. Opin. Microbiol. 3 197–202 Occurrence Handle10745003 Occurrence Handle1:CAS:528:DC%2BD3cXivFajtbY%3D

    PubMed  CAS  Google Scholar 

  61. R. J. Ellis (1997) Curr. Biol. 7 R531–R533 Occurrence Handle9285706 Occurrence Handle1:CAS:528:DyaK2sXmsVSju7o%3D

    PubMed  CAS  Google Scholar 

  62. J. Martin (2002) Biochemistry 41 5050–5055 Occurrence Handle11939802 Occurrence Handle1:CAS:528:DC%2BD38Xhsl2nsbg%3D

    PubMed  CAS  Google Scholar 

  63. B. Berg ParticleVan den R. Wain C. M. Dobson R. J. Ellis (2000) EMBO J. 19 3870–3875 Occurrence Handle10921869

    PubMed  Google Scholar 

  64. P. H. Yancey G. N. Somero (1979) Biochem. J. 183 317–323 Occurrence Handle534499 Occurrence Handle1:CAS:528:DyaL3cXht1Gntrg%3D

    PubMed  CAS  Google Scholar 

  65. P. H. Yancey M. E. Clark S. C. Hand R. D. Bowlus G. N. Somero (1982) Science 217 1214–1222 Occurrence Handle1:CAS:528:DyaL38XlsFyisbw%3D Occurrence Handle7112124

    CAS  PubMed  Google Scholar 

  66. A. Wang D. W. Bolen (1997) Biochemistry 36 9101–9108 Occurrence Handle9230042 Occurrence Handle1:CAS:528:DyaK2sXktleltLg%3D

    PubMed  CAS  Google Scholar 

  67. D. W. Bolen I. V. Baskakov (2001) J. Mol. Biol. 310 955–963 Occurrence Handle11502004 Occurrence Handle1:CAS:528:DC%2BD3MXmslShtbo%3D

    PubMed  CAS  Google Scholar 

  68. M. B. Burg E. M. Peters (1997) Am. J. Physiol. 273 F1048–F1053 Occurrence Handle9435695 Occurrence Handle1:CAS:528:DyaK1cXjsFantg%3D%3D

    PubMed  CAS  Google Scholar 

  69. I. V. Baskakov D. W. Bolen (1998) Biophys. J. 74 2658–2665 Occurrence Handle9591689 Occurrence Handle1:CAS:528:DyaK1cXislWku74%3D

    PubMed  CAS  Google Scholar 

  70. I. V. Baskakov D. W. Bolen (1998) J. Biol. Chem. 273 4831–4834 Occurrence Handle9478922 Occurrence Handle1:CAS:528:DyaK1cXhs1CgtLo%3D

    PubMed  CAS  Google Scholar 

  71. Y. Liu D. W. Bolen (1995) Biochemistry 34 12884–12891 Occurrence Handle7548045 Occurrence Handle1:CAS:528:DyaK2MXnvFGqt7Y%3D

    PubMed  CAS  Google Scholar 

  72. T. Mashino I. Fridovich (1987) Arch. Biochem. Biophys. 258 356–360 Occurrence Handle3674879 Occurrence Handle1:CAS:528:DyaL1cXisFKm

    PubMed  CAS  Google Scholar 

  73. F.-G. Meng Y.-D. Park H.-M. Zhou (2001) Int. J. Biochem. Cell Biol. 33 701–709 Occurrence Handle11390278 Occurrence Handle1:CAS:528:DC%2BD3MXktVKltrY%3D

    PubMed  CAS  Google Scholar 

  74. M. M. Satoro Y. Liu S. M. A. Khan L.-X. Hou D. W. Bolen (1992) Biochemistry 31 5278–5283

    Google Scholar 

  75. P. H. Yancey G. N. Somero (1980) J. Exp. Zool. 212 205–213 Occurrence Handle1:CAS:528:DyaL3cXkvFSqurs%3D

    CAS  Google Scholar 

  76. Q. Zou B. J. Bennion V. Daggett K. P. Murphy (2002) J. Am. Chem. Soc. 124 1192–1202 Occurrence Handle11841287 Occurrence Handle1:CAS:528:DC%2BD38XntlCrug%3D%3D

    PubMed  CAS  Google Scholar 

  77. K. E. Shearwin D. J. Winzor (1988) Biophys. Chem. 31 287–294 Occurrence Handle3233302 Occurrence Handle1:CAS:528:DyaL1MXjs1Sqtg%3D%3D

    PubMed  CAS  Google Scholar 

  78. J. R. Cann R. O. Coombs G. R. Howlett M. P. Jacobsen D. J. Winzor (1994) Biochemistry 33 10185–10190 Occurrence Handle8060984 Occurrence Handle1:CAS:528:DyaK2cXltVensrc%3D

    PubMed  CAS  Google Scholar 

  79. N. A. Chebotareva S. E. Harding D. J. Winzor (2001) Eur. J. Biochem. 268 506–513 Occurrence Handle11168388 Occurrence Handle1:CAS:528:DC%2BD3MXht1Gnt70%3D

    PubMed  CAS  Google Scholar 

  80. N. A. Chebotareva I. E. Andreeva V. F. Makeeva B. I. Kurganov N. B. Livanova S. E. Harding (2002) Progr. Colloid. Polym. Sci. 119 70–76 Occurrence Handle1:CAS:528:DC%2BD38Xhtl2kurY%3D Occurrence Handle10.1007/3-540-44672-9_11

    Article  CAS  Google Scholar 

  81. M. R. Carner D. C. Rau (1995) EMBO J. 14 1257–1263

    Google Scholar 

  82. J. Poon M. Bailey D. J. Winzor B. E. Davidson W. H. Sawyer (1997) Biophys. J. 73 3257–3264 Occurrence Handle9414236 Occurrence Handle1:CAS:528:DyaK2sXnsl2lsbw%3D

    PubMed  CAS  Google Scholar 

  83. C. N. Patel S. M. Noble G. T. Weatherly A. Tripathy D. J. Winzor G. J. Pielak (2002) Prot. Sci. 11 997–1003 Occurrence Handle1:CAS:528:DC%2BD38Xjt12itr0%3D

    CAS  Google Scholar 

  84. P. R. Wills M. P. Jacobsen D. J. Winzor (1996) Biopolymers 38 119–130 Occurrence Handle1:CAS:528:DyaK28XpvVem

    CAS  Google Scholar 

  85. A. G. Ogston D. J. Winzor (1975) J. Phys. Chem. 79 2496–2500 Occurrence Handle1:CAS:528:DyaE2MXmtV2qt7c%3D

    CAS  Google Scholar 

  86. L. W. Nichol P. D. Jeffrey D. J. Winzor (1976) J. Phys. Chem. 80 648–649 Occurrence Handle1:CAS:528:DyaE28XhtFajsrg%3D

    CAS  Google Scholar 

  87. F.-G. Meng Y.-K. Hong H.-W. He A. E. Lyubarev B. I. Kurganov Y.-B. Yan H.-M. Zhou (2004) Biophys. J. 87 2247–2254 Occurrence Handle15454427 Occurrence Handle1:CAS:528:DC%2BD2cXot12nu7w%3D

    PubMed  CAS  Google Scholar 

  88. A. S. Morar A. Olteanu G. B. Young G. J. Pielak (2001) Prot. Sci. 10 2195–2199 Occurrence Handle1:CAS:528:DC%2BD3MXnvV2rsrw%3D

    CAS  Google Scholar 

  89. A. J. Saunders P. R. Davis-Searles D. L. Allen G. J. Pielak D. A. Erie (2000) Biopolymers 53 293–307 Occurrence Handle10685050 Occurrence Handle1:CAS:528:DC%2BD3cXhs12rsbc%3D

    PubMed  CAS  Google Scholar 

  90. T. G. A. Lonhienne D. J. Winzor (2001) Biochemistry 40 9618–9622 Occurrence Handle11583161 Occurrence Handle1:CAS:528:DC%2BD3MXkvFCrtb0%3D

    PubMed  CAS  Google Scholar 

  91. T. G. A. Lonhienne D. J. Winzor (2002) Biochemistry 41 6897–6901 Occurrence Handle12033921 Occurrence Handle1:CAS:528:DC%2BD38XjtlOhurc%3D

    PubMed  CAS  Google Scholar 

  92. D. E. Koshland G. Nemethy D. Filmer (1966) Biochemistry 5 365–385 Occurrence Handle5938952 Occurrence Handle1:CAS:528:DyaF28XivVGnsw%3D%3D

    PubMed  CAS  Google Scholar 

  93. G. T. Weatherly G. J. Pielak (2001) Prot. Sci. 10 12–16 Occurrence Handle1:CAS:528:DC%2BD3MXksFCjtbY%3D

    CAS  Google Scholar 

  94. M. P. Jacobsen P. R. Wills D. J. Winzor (1996) Biochemistry 35 13173–13179 Occurrence Handle8855955 Occurrence Handle1:CAS:528:DyaK28Xls1egt7g%3D

    PubMed  CAS  Google Scholar 

  95. D. R. Hall M. P. Jacobsen D. J. Winzor (1995) Biophys. Chem. 57 47–54 Occurrence Handle8534836 Occurrence Handle1:CAS:528:DyaK2MXos1Ggsrk%3D

    PubMed  CAS  Google Scholar 

  96. P. R. Wills D. R. Hall D. J. Winzor (2000) Biophys. Chem. 84 217–225 Occurrence Handle10852309 Occurrence Handle1:CAS:528:DC%2BD3cXjt1eis78%3D

    PubMed  CAS  Google Scholar 

  97. S. N. Timasheff (1992) Biochemistry 31 9857–9864 Occurrence Handle1390769 Occurrence Handle1:CAS:528:DyaK38XlvVKrt74%3D

    PubMed  CAS  Google Scholar 

  98. S. N. Timasheff (1993) Annu. Rev. Biophys. Biochem. Struct. 22 67–97 Occurrence Handle1:CAS:528:DyaK3sXlsFCjurk%3D

    CAS  Google Scholar 

  99. T. Arakawa R. Bhat S. N. Timasheff (1985) Biophys. J. 47 411–414 Occurrence Handle3978211 Occurrence Handle1:CAS:528:DyaL2MXhs1antb4%3D

    PubMed  CAS  Google Scholar 

  100. I. V. Baskakov D. W. Bolen (1998) Biophys. J. 74 2666–2673 Occurrence Handle9591690 Occurrence Handle1:CAS:528:DyaK1cXislWku78%3D Occurrence Handle10.1016/S0006-3495(98)77972-X

    Article  PubMed  CAS  Google Scholar 

  101. Y. Qu C. L. Bolen D. W. Bolen (1998) Proc. Natl. Acad. Sci. USA 95 9268–9279 Occurrence Handle9689069 Occurrence Handle1:CAS:528:DyaK1cXltlCmtbc%3D

    PubMed  CAS  Google Scholar 

  102. H. R. Palmer J. J. Bedford J. P. Leader R. A. J. Smith (2000) J. Biol. Chem. 36 27708–27711

    Google Scholar 

  103. J. C. Lee K. Gekko S. N. Timashev (1979) Meth. Enzymol. 61 26–49 Occurrence Handle10.1016/0076-6879(79)61005-4 Occurrence Handle481227 Occurrence Handle1:CAS:528:DyaE1MXmtVKms78%3D

    Article  PubMed  CAS  Google Scholar 

  104. D. L. Sackett (1997) Am. J. Physiol. 273 R669–R676 Occurrence Handle9277553 Occurrence Handle1:CAS:528:DyaK2sXls12gtbg%3D

    PubMed  CAS  Google Scholar 

  105. D.-S. Yang C. M. Yip T. H. J. Huang A. Chakrabatty (1999) J. Biol. Chem. 274 32970–32974 Occurrence Handle10551864 Occurrence Handle1:CAS:528:DyaK1MXntlygurw%3D

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia

    N. A. Chebotareva, B. I. Kurganov & N. B. Livanova

Authors
  1. N. A. Chebotareva
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. B. I. Kurganov
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. N. B. Livanova
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to N. A. Chebotareva.

Additional information

Translated from Biokhimiya, Vol. 69, No. 11, 2004, pp. 1522–1536.

Original Russian Text Copyright © 2004 by Chebotareva, Kurganov, Livanova.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chebotareva, N.A., Kurganov, B.I. & Livanova, N.B. Biochemical effects of molecular crowding. Biochemistry (Moscow) 69, 1239–1251 (2004). https://doi.org/10.1007/s10541-005-0070-y

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10541-005-0070-y

Key word

Search

Navigation