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DOI: 10.1039/C6CC90360F (Correction) Chem. Commun., 2016, 52, 10440-10441

Correction: A narrow amide I vibrational band observed by sum frequency generation spectroscopy reveals highly ordered structures of a biofilm protein at the air/water interface

Zhuguang Wang a, M. Daniela Morales-Acosta b, Shanghao Li c, Wei Liu a, Tapan Kanai a, Yuting Liu a, Ya-Na Chen a, Frederick J. Walker b, Charles H. Ahn b, Roger M. Leblanc c and Elsa C. Y. Yan *a
aDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, USA. E-mail: elsa.yan@yale.edu
bDepartment of Applied Physics, Yale University, 15 Prospect Street, New Haven, Connecticut 06520, USA
cDepartment of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA

Received 28th July 2016 , Accepted 28th July 2016

First published on 4th August 2016

Abstract

Correction for ‘A narrow amide I vibrational band observed by sum frequency generation spectroscopy reveals highly ordered structures of a biofilm protein at the air/water interface’ by Zhuguang Wang et al., Chem. Commun., 2016, 52, 2956–2959.

In follow-up studies by the authors, it was found that due to an inaccuracy in calibration of spectrometer, there should be a blue-shift of 7 cm−1 in the peak positions of the SFG spectra published in this article. The new peak positions allowed more straightforward spectral assignments of the reported SFG spectral based on the standard amide I frequencies of various protein secondary structures.1,2 The chiral SFG spectrum of BslA at pH = 7.4 (Fig. 1D) is now assigned to antiparallel β-sheet B2 mode (1637 cm−1) and β-turn (1663 cm−1). The peak assignments in the achiral spectra (Fig. 1C and E) remain unchanged: β-turn (1676 cm−1) and antiparallel β-sheet B1 mode (1692 cm−1). The recalibrated spectra (Fig. 1C–F) and fitting parameters are provided below. The conclusion of the studies reported in the article remains unaffected.
image file: c6cc90360f-f1.tif
Fig. 1 (C) Achiral (ssp) and (D) chiral (psp) SFG spectra of BslA at the air/water interface at pH 7.4 with a concentration of 6 μM. (E) Achiral (ssp) and (F) chiral (psp) SFG spectra of BslA at pH 1.2 with a bulk concentration of 6 μM.
Table 1 Fitting parameters of achiral and chiral SFG spectra for BslA
Parameters Amide I (achiral-ssp)

Fig. 1C (pH 7.4)
χ NR (a.u.) 0.020 ± 0.005
ω (cm−1) 1675.5 ± 0.7 1692.3 ± 0.4
A (a.u.) 1.99 ± 0.24 0.53 ± 0.16
Γ (a.u.) 11.75 ± 1.29 5.25 ± 1.09
Parameters Amide I (chiral-psp)

Fig. 1D (pH 7.4)

 Amide I (achiral-ssp)

Fig. 1E (pH 1.2)
χ NR (a.u.) 0.056 ± 0.004 −0.005 ± 0.003
ω (cm−1) 1636.8 ± 2.8 1662.5 ± 3.9 1675.6 ± 0.8
A (a.u.) 1.71 ± 0.87 −1.97 ± 0.87 3.97 ± 0.10
Γ (a.u.) 19.92 ± 4.78 23.35 ± 4.79 20.15 ± 0.62

The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.

References

  1. L. K. Tamm and S. A. Tatulian, Infrared Spectroscopy of Proteins and Peptides in Lipid Bilayers, Q. Rev. Biophys., 1997, 30, 365–429 CrossRef CAS PubMed.
  2. A. Barth and C. Zscherp, What Vibrations Tell Us About Proteins, Q. Rev. Biophys., 2002, 35, 369–430 CrossRef CAS PubMed.
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