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Conformation of a T cell stimulating peptide in aqueous solution
Author(s) -
Waltho Jonathan P.,
Feher Victoria A.,
Lerner Richard A.,
Wright Peter E.
Publication year - 1989
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(89)80764-1
Subject(s) - circular dichroism , aqueous solution , myoglobin , chemistry , peptide , folding (dsp implementation) , nuclear magnetic resonance spectroscopy , crystallography , sperm whale , protein folding , protein secondary structure , biophysics , stereochemistry , biochemistry , biology , electrical engineering , engineering
Using two‐dimensional NMR spectroscopy and circular dichroism spectroscopy it is demonstrated that a T cell stimulating peptide corresponding to residues 132–153 of sperm whale myoglobin populates helical conformations in aqueous solution. This finding is in accordance with proposals that immunodominant sites in T cell stimulating peptides have a high conformational propensity. The observation of secondary structure in aqueous solutions of this and other immunogenic peptides has important implications for initiation of protein folding.