A gradual disruption of tight side-chain packing:: 2D 1H-NMR characterization of acid-induced unfolding of CHABII

被引：32

作者：

Song, JX ^{[1
]}

Jamin, N ^{[1
]}

Gilquin, B ^{[1
]}

Vita, C ^{[1
]}

Ménez, A ^{[1
]}

机构：

[1] CEA, Dept Ingn & Etud Prot, F-91191 Gif Sur Yvette, France

来源：

NATURE STRUCTURAL BIOLOGY | 1999年 / 6卷 / 02期

关键词：

D O I：

10.1038/5815

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：

Little is known about the mechanism of the transition between native proteins and partially folded intermediates. Complete assignments of 2D H-1-NOESY spectra of CHABII at 5 degrees C, pH 6.3, 5.5, 4.6 and 4.0, reveal that lowering of pH results in an extensive but gradual disappearance of NOEs, implying a gradual disruption of tight side-chain packing. Moreover, a tertiary packing core is identified at 5 degrees C and pH 4.0, characterized by persistent long-range NOEs, Thus, we suggest that severe disruption of tight side-chain packing of CHABII can occur at a stage where its secondary structure and tertiary topology remain highly native-like.

引用

页码：129 / 134

页数：6

共 38 条

[1] On-pathway versus off-pathway folding intermediates [J].

Baldwin, RL .

FOLDING & DESIGN, 1996, 1 (01) :R1-R8

[2] MOLECULAR MECHANISMS OF ACID DENATURATION - THE ROLE OF HISTIDINE-RESIDUES IN THE PARTIAL UNFOLDING OF APOMYOGLOBIN [J].

BARRICK, D ;

HUGHSON, FM ;

BALDWIN, RL .

JOURNAL OF MOLECULAR BIOLOGY, 1994, 237 (05) :588-601

[3] DE-NOVO PROTEIN DESIGN - FROM MOLTEN GLOBULES TO NATIVE-LIKE STATES [J].

BETZ, SF ;

RALEIGH, DP ;

DEGRADO, WF .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1993, 3 (04) :601-610

[4] REFINED STRUCTURE OF CHARYBDOTOXIN - COMMON MOTIFS IN SCORPION TOXINS AND INSECT DEFENSINS [J].

BONTEMS, F ;

ROUMESTAND, C ;

GILQUIN, B ;

MENEZ, A ;

TOMA, F .

SCIENCE, 1991, 254 (5037) :1521-1523

[5] SOLUTION STRUCTURE OF GAMMA-1-H AND GAMMA-1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY H-1-NMR - A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS [J].

BRUIX, M ;

JIMENEZ, MA ;

SANTORO, J ;

GONZALEZ, C ;

COLILLA, FJ ;

MENDEZ, E ;

RICO, M .

BIOCHEMISTRY, 1993, 32 (02) :715-724

[6] Solution structure of the thermostable sweet-tasting protein brazzein [J].

Caldwell, JE ;

Abildgaard, F ;

Dzakula, Z ;

Ming, D ;

Hellekant, G ;

Markley, JL .

NATURE STRUCTURAL BIOLOGY, 1998, 5 (06) :427-431

[7] On the convergent evolution of animal toxins - Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures [J].

Dauplais, M ;

Lecoq, A ;

Song, JX ;

Cotton, J ;

Jamin, N ;

Gilquin, B ;

Roumestand, C ;

Vita, C ;

deMedeiros, CLC ;

Rowan, EG ;

Harvey, AL ;

Menez, A .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (07) :4302-4309

[8] ASSIGNMENT OF COMPLEX H-1-NMR SPECTRA VIA TWO-DIMENSIONAL HOMONUCLEAR HARTMANN-HAHN SPECTROSCOPY [J].

DAVIS, DG ;

BAX, A .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1985, 107 (09) :2820-2821

[9] Kinetic studies of protein folding using NMR spectroscopy [J].

Dobson, CM ;

Hore, PJ .

NATURE STRUCTURAL BIOLOGY, 1998, 5 (Suppl 7) :504-507

[10] Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation [J].

Drakopoulou, E ;

Vizzavona, J ;

Neyton, J ;

Aniort, V ;

Bouet, F ;

Virelizier, H ;

Ménez, A ;

Vita, C .

BIOCHEMISTRY, 1998, 37 (05) :1292-1301

← 1 2 3 4 →