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Effect of temperature on the circular dichroism spectra of β 2 ‐microglobulins
Author(s) -
Brown Eleanor M.,
Groves Merton L.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80647-5
Subject(s) - circular dichroism , chemistry , tyrosine , crystallography , residue (chemistry) , conformational change , vibrational circular dichroism , stereochemistry , biochemistry
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 β 2 ‐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 Δ H ° 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 sequence.