Librational motion of an "immobilized" spin label: hemoglobin spin labeled by a maleimide derivative.

Abstract:

:The spin label Tempo-maleimide, when "immobilized" in hemoglobin, is shown to exhibit motional fluctuation whose amplitude and/or frequency depend on temperature and solution conditions. These motional fluctuations are observable by several electron spin resonance techniques. For desalted hemoglobin the fluctuations are detectable at approximately -15 degrees C using saturation transfer techniques and at approximately +25 degrees C using line-width measurements of normal absorption spectra. In ammonium sulfate precipitated hemoglobin, however, motional fluctuations are not detectable by either technique up to at least 40 degrees C. The most probable mechanism for spin-label motion appears to be either fluctuations in protein conformation which affect the label binding site or conformational transitions of the nitroxide ring itself. These motional fluctuations are shown to introduce a librational character to the overall label motion during hemoglobin rotational diffusion, with the librational motion significantly affecting the use of spin-label spectral shapes to calculate hemoglobin rotational correlation times.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Johnson ME

doi

10.1021/bi00600a014

subject

Has Abstract

pub_date

1978-04-04 00:00:00

pages

1223-8

issue

7

eissn

0006-2960

issn

1520-4995

journal_volume

17

pub_type

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