Effect of temperature on the circular dichroism spectra of β2‐microglobulins
Authors:
- Eleanor M. BrownEBEleanor M. Brown
- Merton L. GrovesMGMerton L. Groves
- 6 May 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 184 (1) , 36-39
Abstract
When the temperature was lowered from 25 to 5°C dramatic changes were observed in the near-ultraviolet circular dichroism spectra of bovine and caprine but not human β2-imcroglobulin. Comparison of the protein sequences suggests that the conformational change occurs in the amino-terminal 24 residues and that a tyrosine residue located on a potential β-turn acts as a reporter group. Because ΔH° is small (−22 kcal · mol−1), such conformational changes, possibly not readily observed, may occur at low temperatures in other proteins having potential β-turns in otherwise aperiodic regions of sequenceKeywords
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