PROBING PROTEIN-STRUCTURE BY SOLVENT PERTURBATION OF NMR-SPECTRA - PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION AND PARAMAGNETIC PERTURBATION TECHNIQUES APPLIED TO THE STUDY OF THE MOLTEN GLOBULE STATE OF ALPHA-LACTALBUMIN

被引：25

作者：

IMPROTA, S

MOLINARI, H

PASTORE, A

CONSONNI, R

ZETTA, L

机构：

[1] CNR,CTR STUDI BIOPOLIMERI,PADUA,ITALY

[2] UNIV VERONA,IST POLICATTEDRA,VERONA,ITALY

[3] CNR,IST CHIM MACROMOLEC,NMR LAB,MILAN,ITALY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1995年 / 227卷 / 1-2期

关键词：

SURFACE MAPPING; NMR; PHOTO-CIDNP; TEMPOL; PROTEIN FOLDING;

D O I：

10.1111/j.1432-1033.1995.tb20362.x

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：

We have characterized the high-temperature molten globule state of bovine alpha-lactalbumin by a combined use of photochemically induced dynamic nuclear polarization and nitroxide surface perturbation. Both techniques are extremely well suited to follow the progressive increase of exposed surfaces in the native state and the appearance of partially or completely unfolded species. Our results suggest that the molten globule state obtained at high temperature and pH 7, and the state obtained at pH 2 are not only thermodynamically but also structurally very similar.

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页码：87 / 96

页数：10

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