Erratum: “Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. I. GVGGR and GMGGQ repeats”, Volume 49, No. 4, pp. 303–312 (1999)

✍ Scribed by Guangzhao Xu; John Spencer Evans

• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 28 KB
• Volume: 50
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(199909)50:3<345::aid-bip9>3.0.co;2-b

✦ Synopsis

We wish to report two corrections to our article which appeared in Biopolymers Vol. 49,[303][304][305][306][307][308][309][310][311][312] 1999. First, throughout the text, we erroneously used the definitions d N␣(i,iϩ1) , d N␣(i,iϩ2) , d N␣(i,iϩ3) to indicate rOe magnetization transfer between CH ␣ and NH ␣ protons; these definitions should read as d ␣N(i,iϩ1) , d ␣N(i,iϩ2) , d ␣N(i,iϩ3) , as defined by Wuthrich and co-workers (J. Mol. Biology, 187, 131-135, 1986). Second, in Figure 1, we discovered that we incorrectly calculated the values of ⌬␦H ␣ ; in our original paper, we subtracted our observed ⌬␦H ␣ values from the ⌬␦H ␣ "random coil" values. In fact, ⌬␦H ␣ ϭ ␦H ␣,observed Ϫ ␦H ␣,"random coil" (J. Mol. Biology, 222,. Hence, our original ⌬␦H ␣ values were correct in terms of magnitude, but incorrect in terms of (ϩ) and (Ϫ) sign. This error has now been corrected, and the revised Figure 1 is presented herein. Based upon the revised Figure 1, our qualitative interpretations of the ⌬␦H ␣ values remain unchanged: the 23-mer SM50 peptidomimetic exists in a nonextended conformation. However, since most of the ⌬␦H ␣ values are positive, we would amend our statements at the end of the section, "CH ␣ Conformational Shifts" (p. 306), to read as follows: "As observed in Figure 1, all residues, with the exception of Gln and Pro, are downfield shifted. These findings provide qualitative evidence for a nonextended conformation consistent with a ␤-strand structure with partial ␤-turn or ␣-helical content.