How do cofactors modulate protein folding?

被引：15

作者：

Higgins, CL

Muralidhara, BK

Wittung-Stafshede, P

机构：

[1] Rice Univ, Dept Biochem & Cell Biol, Houston, TX 77251 USA

[2] Tulane Univ, Dept Chem, New Orleans, LA 70118 USA

来源：

PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 02期

关键词：

cofactor-binding protein; azurin; flavodoxin; ferredoxin; flavin mononucleotide; iron-sulfur cluster; folding speed; folding pathway;

D O I：

10.2174/0929866053005782

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cofactors are essential components of many proteins for biological activity. Characterization of several cofactor-binding proteins has shown that cofactors often have the ability to interact specifically with the unfolded polypeptides. This suggests that cofactor-coordination prior to polypeptide folding may be a relevant path in vivo. By binding before folding, the cofactor may affect both the mechanism and speed of folding. Here, we discuss three different cofactors that modulate protein-folding processes in vitro.

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页码：165 / 170

页数：6

相关论文

共 48 条

[1]

ADMAN ET, 1991, ADV PROTEIN CHEM, V42, P145

[2] Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin [J].

Apiyo, D ;

Wittung-Stafshede, P .

PROTEIN SCIENCE, 2002, 11 (05) :1129-1135

[3] Iron-sulfur clusters: Nature's modular, multipurpose structures [J].

Beinert, H ;

Holm, RH ;

Munck, E .

SCIENCE, 1997, 277 (5326) :653-659

[4] Structural and dynamical properties of a partially unfolded Fe4S4 protein:: Role of the cofactor in protein folding [J].

Bentrop, D ;

Bertini, I ;

Iacoviello, R ;

Luchinat, C ;

Niikura, Y ;

Piccioli, M ;

Presenti, C ;

Rosato, A .

BIOCHEMISTRY, 1999, 38 (15) :4669-4680

[5] Characterization of a partially unfolded high potential iron protein [J].

Bertini, I ;

Cowan, JA ;

Luchinat, C ;

Natarajan, K ;

Piccioli, M .

BIOCHEMISTRY, 1997, 36 (31) :9332-9339

[6]

Bertini I., 1994, Bioinorganic Chemistry, DOI 10/BioinCh_chapter9.pdf

[7] Kinetics and thermodynamics of copper(II) binding to apoazurin [J].

Blasie, CA ;

Berg, JM .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (23) :6866-6867

[8] Population statistics of protein structures: Lessons from structural classifications [J].

Brenner, SE ;

Chothia, C ;

Hubbard, TJP .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1997, 7 (03) :369-376

[9] PRIMARY SEQUENCE, OXIDATION-REDUCTION POTENTIALS AND TERTIARY-STRUCTURE PREDICTION OF DESULFOVIBRIO-DESULFURICANS ATCC-27774 FLAVODOXIN [J].

CALDEIRA, J ;

PALMA, PN ;

REGALLA, M ;

LAMPREIA, J ;

CALVETE, J ;

SCHAFER, W ;

LEGALL, J ;

MOURA, I ;

MOURA, JJG .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1994, 220 (03) :987-995

[10] Blotting analysis of native IRP1: A novel approach to distinguish the different forms of IRP1 in cells and tissues [J].

Campanella, A ;

Levi, S ;

Cairo, G ;

Biasiotto, G ;

Arosio, P .

BIOCHEMISTRY, 2004, 43 (01) :195-204

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