SPIN-LATTICE RELAXATION IN THE TRIPLET-STATE OF THE BURIED TRYPTOPHAN RESIDUE OF RIBONUCLEASE-T1

被引：14

作者：

GHOSH, S ^{[1
]}

PETRIN, M ^{[1
]}

MAKI, A ^{[1
]}

机构：

[1] UNIV CALIF DAVIS, DEPT CHEM, DAVIS, CA 95616 USA

来源：

BIOPHYSICAL JOURNAL | 1986年 / 49卷 / 03期

关键词：

D O I：

10.1016/S0006-3495(86)83701-8

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The individual spin-lattice relaxation (SLR) rate constants (Wij) between the lowest triplet sublevels of the lone tryptophan residue buried in the interior of the globular protein ribonulease T1 have been reported in the temperature range 1.2 to 3.0 K in zero applied magnetic field. The SLR rate constants between spin sublevels exhibit marked anisotropy in their magnitudes and also show appreciable sensitivity to the glycerol content of the aqueous cryogenic matrix. The temperature dependence of SLR suggests that in the temperature range investigated a direct process contributes dominantly to the SLR in this protein.

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页码：753 / 760

页数：8

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