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Conformation of Bovine Nerve Root P 2 Protein: Characteristics of the Molecule from Circular Dichroism Spectra
Author(s) -
Weise M. J.,
Brostoff S. W.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb06639.x
Subject(s) - circular dichroism , chemistry , cyanogen bromide , crystallography , peptide , tyrosine , protein folding , molecule , residue (chemistry) , protein structure , urea , stereochemistry , peptide sequence , biochemistry , organic chemistry , gene
Circular dichroism (CD) was used to study the conformations of bovine nerve root P 2 basic protein, its reduced and carboxymethylated derivative (RCM‐P 2 ), and its large cyanogen bromide fragment (CN1). Data in the far UV show that both the parent protein and RCM‐P 2 have conformations dominated by a large amount of β structure. However, the CN1 peptide appears to exist in a largely unordered conformation. Since CN1 lacks short (20 residue) amino‐ and carboxy‐terminal segments of the P 2 protein, the spectral data suggest that these regions are important for determining and/or maintaining folding of the P 2 protein in aqueous solutions. The P 2 protein was found to have a distinctive CD spectrum in the near UV. The characteristics of molar ellipticities indicate that the spectrum contains significant contributions from tyrosine residues, and that these contributions suggest different environments for the two tyrosines in P 2 protein. Both environments depend on protein conformation, since CD side chain absorptions are lost when P 2 protein is denatured with 5 M urea.