Cooperativity, connectivity, and folding pathways of multidomain proteins.
Multidomain proteins are ubiquitous in both prokaryotic and eukaryotic proteomes. Study on protein folding, however, has concentrated more on the isolated single domains of proteins, and there have been relatively few systematic studies on the effects of domain-domain interactions on folding. We here discuss this issue by examining human gammaD-crystallin, spore coat protein S, and a tandem array of the R16 and R17 domains of spectrin as example proteins by using a structure-based model of folding. The calculated results consistently explain the experimental data on folding pathways and effects of mutational perturbations, supporting the view that the connectivity of two domains and the distribution of domain-domain interactions in the native conformation are factors to determine kinetic and equilibrium properties of cooperative folding.
Itoh
Kazuhito
K
Department of Computational Science and Engineering, Nagoya University, Nagoya 464-8603, Japan. kazuhito@tbp.cse.nagoya-u.ac.jp
Sasai
Masaki
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D003459:Crystallins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013049:Spectrin / Q000737:chemistry* / Q000378:metabolism*; D038222:gamma-Crystallins
D001426:Bacterial Proteins; C504903:CRYGD protein, human; D003459:Crystallins; D038222:gamma-Crystallins; C024278:protein S, Myxococcus xanthus; D013049:Spectrin
Protein Sci. 2003 Mar;12(3):480-90
12592018
J Mol Biol. 2005 Jun 24;349(5):1045-59
15913648
J Biol Chem. 2006 Oct 13;281(41):30782-93
16891314
Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10141-6
16006532
Biopolymers. 2003 Mar;68(3):333-49
12601793
Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13014-8
11606790
J Mol Biol. 2005 Dec 2;354(3):679-92
16257414
Phys Rev Lett. 2002 Jun 24;88(25 Pt 1):258101
12097132
Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14736-41
15466708
J Mol Biol. 2004 Jun 11;339(4):951-65
15165862
Protein Sci. 2005 Mar;14(3):569-81
15722442
Proc Natl Acad Sci U S A. 2006 Jan 17;103(3):586-91
16407126
Curr Opin Struct Biol. 2008 Feb;18(1):27-34
18243686
Phys Rev Lett. 2006 Aug 11;97(6):068106
17026210
Biopolymers. 1981 May;20(5):991-1011
7225531
Curr Opin Struct Biol. 2004 Feb;14(1):70-5
15102452
J Mol Biol. 2005 Mar 4;346(4):1121-45
15701522
J Mol Biol. 2001 Aug 24;311(4):879-90
11518537
Annu Rev Phys Chem. 1997;48:545-600
9348663
J Mol Biol. 2006 Jun 16;359(4):1075-85
16678203
Biophys J. 2006 Mar 15;90(6):2120-30
16387757
J Mol Biol. 2003 Feb 21;326(3):933-54
12581651
FEBS Lett. 1998 Oct 30;438(1-2):127-30
9821973
Phys Rev Lett. 2007 Jul 20;99(3):038103
17678333
Proc Natl Acad Sci U S A. 2006 May 9;103(19):7298-303
16648265
Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11311-6
10500173
Eur J Biochem. 1998 Aug 1;255(3):604-10
9738899
J Mol Biol. 2004 Nov 12;344(1):195-205
15504411
Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1489-93
18230738
Nat Rev Mol Cell Biol. 2007 Apr;8(4):319-30
17356578
Protein Sci. 2005 Aug;14(8):2030-43
16046626
Protein Sci. 2002 Oct;11(10):2351-61
12237457
PLoS Comput Biol. 2008 May 16;4(5):e1000070
18483553
Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9202-6
12082180
Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):511-6
14694192
Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17747-52
17095606
Protein Sci. 2007 Nov;16(11):2427-44
17905830
Protein Sci. 2004 Aug;13(8):2223-35
15273315
Biochemistry. 2001 Apr 3;40(13):3974-84
11300778
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3352-7
14988499
Phys Rev Lett. 2007 Apr 6;98(14):148102
17501316