Dynamics of a protein matrix revealed by fluorescence quenching.

Abstract:

:The fluorescence of the supposedly buried tryptophan in ribonuclease T1 has been found to be collisionally quenched by acrylamide with a rate constant of 3 X 10(8) M--1 sec--1. Only a slight decrease in the quenching rate is observed upon a 5-fold increase in the viscosity of the solution. For this to be the case, the diffusion of the quencher must be limited by the protein matrix. To explain the process of diffusion through this complex material, the formation of "holes" in the lattice of a protein due to nanosecond fluctuations must be invoked. Thus, the dynamic character of a protein molecule is revealed. The quenching rate constant has an activation energy of 9 kcal/mol which can be used to characterize the nature of the cohesive forces in the microenvironment about the indole ring. The mechanical properties of a portion of a protein matrix can, therefore, be described as one would for a fluid.

authors

Eftink MR,Ghiron CA

doi

10.1073/pnas.72.9.3290

subject

Has Abstract

pub_date

1975-09-01 00:00:00

pages

3290-4

issue

9

eissn

0027-8424

issn

1091-6490

journal_volume

72

pub_type

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