Protein folding in confined and crowded environments.
Confinement and crowding are two major factors that can potentially impact protein folding in cellular environments. Theories based on considerations of excluded volumes predict disparate effects on protein folding stability for confinement and crowding: confinement can stabilize proteins by over 10k(B)T but crowding has a very modest effect on stability. On the other hand, confinement and crowding are both predicted to favor conformations of the unfolded state which are compact, and consequently may increase the folding rate. These predictions are largely borne out by experimental studies of protein folding under confined and crowded conditions in the test tube. Protein folding in cellular environments is further complicated by interactions with surrounding surfaces and other factors. Concerted theoretical modeling and test-tube and in vivo experiments promise to elucidate the complexity of protein folding in cellular environments.
Zhou
Huan-Xiang
HX
Department of Physics and Institute of Biophysics and School of Computational Science, Florida State University, Tallahassee, FL 32306, USA. zhou@sb.fsu.edu
D008962:Models, Theoretical; D017510:Protein Folding; D013816:Thermodynamics
J Mol Recognit. 2004 Sep-Oct;17(5):368-75
15362094
J Am Chem Soc. 2006 Mar 29;128(12):3916-7
16551092
Protein Sci. 2005 May;14(5):1125-33
15802645
Protein Sci. 2004 Jan;13(1):125-33
14691228
Biophys J. 2005 Feb;88(2):971-85
15596487
J Mol Biol. 1998 Apr 10;277(4):985-94
9545386
Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics. 1996 Aug;54(2):1134-1152
9965182
J Chem Phys. 2007 Dec 28;127(24):245101
18163710
Biol Chem. 2006 May;387(5):485-97
16740119
Biopolymers. 2007;88(2):157-63
17206628
Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics. 1999 Jun;59(6):6853-78
11969674
Protein Expr Purif. 2005 Jul;42(1):173-7
15939304
J Am Chem Soc. 2006 Nov 22;128(46):14782-3
17105269
Adv Exp Med Biol. 2007;594:1-13
17205670
J Am Chem Soc. 2004 Oct 6;126(39):12224-5
15453729
J Cell Sci. 2006 Jul 15;119(Pt 14):2863-9
16825427
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3535-9
11904417
J Mol Biol. 2004 Feb 6;336(1):203-12
14741216
Biochemistry. 2001 Sep 25;40(38):11289-93
11560476
Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11615-7
8876184
J Am Chem Soc. 2006 May 17;128(19):6316-7
16683786
Langmuir. 2005 Nov 8;21(23):10632-7
16262330
Protein Sci. 2004 Mar;13(3):822-9
14978313
Biophys Chem. 2002 Dec 10;101-102:155-65
12487997
Nano Lett. 2006 May;6(5):901-5
16683822
Acc Chem Res. 2004 Feb;37(2):123-30
14967059
J Mol Biol. 2006 Aug 4;361(1):7-10
16824541
Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18956-61
16357202
J Mol Biol. 2006 Feb 3;355(5):893-7
16343531
Nat Struct Mol Biol. 2004 Apr;11(4):352-7
14990997
J Mol Biol. 2007 Jan 19;365(3):856-69
17084857
Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10430-4
17563390
Phys Rev Lett. 2006 Oct 27;97(17):178302
17155512
J Am Chem Soc. 2006 Aug 2;128(30):9580-1
16866482
Cell. 2006 Jun 2;125(5):903-14
16751100
Biochemistry. 2006 Nov 7;45(44):13356-60
17073456
Curr Biol. 2006 Apr 18;16(8):R269-71
16631567
J Mol Biol. 2005 Aug 5;351(1):219-32
15992823
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2399-406
11226251
Nat Struct Mol Biol. 2005 Dec;12(12):1123-9
16299515
J Am Chem Soc. 2004 Aug 11;126(31):9498-9
15291527
Phys Rev Lett. 1988 Nov 21;61(21):2496-2499
10039133
J Phys Chem B. 2006 Jun 22;110(24):11615-9
16800453
Biochemistry. 2004 Mar 2;43(8):2141-54
14979710