Methods to study protein folding by stopped-flow FT-IR - PubMed

Review

Methods to study protein folding by stopped-flow FT-IR

Heinz Fabian et al. Methods. 2004 Sep.

Abstract

Stopped-flow mixing coupled with time-resolved Fourier transform infrared (FT-IR) spectroscopy represents a new experimental approach to explore protein folding events, which has become possible only recently with the development of appropriate techniques. Here, we discuss experimental apparatus that are capable of initiating and monitoring protein folding processes on the millisecond to minute timescale. The strongest point of the FT-IR approach as a structure-specific probe is that a complete spectrum is available for each time point of measurement. In this way, several spectral windows are accessible simultaneously for the observation of the unfolding or the formation of different secondary structure elements and also events that can be attributed to changes in tertiary structure. One specific advantage of the infrared technique is the ability to monitor directly the kinetics of processes involving beta-sheet structures, which is exceptionally difficult to do with other techniques.

Similar articles

• Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.

  Reinstädler D, Fabian H, Backmann J, Naumann D. Reinstädler D, et al. Biochemistry. 1996 Dec 10;35(49):15822-30. doi: 10.1021/bi961810j. Biochemistry. 1996. PMID: 8961946

• Analytical applications of Fourier transform-infrared (FT-IR) spectroscopy in microbiology and prion research.

  Beekes M, Lasch P, Naumann D. Beekes M, et al. Vet Microbiol. 2007 Aug 31;123(4):305-19. doi: 10.1016/j.vetmic.2007.04.010. Epub 2007 Apr 8. Vet Microbiol. 2007. PMID: 17540519 Review.

• Temperature-induced unfolding of ribonuclease A embedded in spherical polyelectrolyte brushes.

  Wittemann A, Ballauff M. Wittemann A, et al. Macromol Biosci. 2005 Jan 14;5(1):13-20. doi: 10.1002/mabi.200400133. Macromol Biosci. 2005. PMID: 15633159

• [Studies on dynamics of protein folding/unfolding by using the laser-induced temperature jump technique].

  Mizutani Y, Yamamoto K, Kitagawa T. Mizutani Y, et al. Tanpakushitsu Kakusan Koso. 2002 May;47(6):670-6. Tanpakushitsu Kakusan Koso. 2002. PMID: 11995333 Review. Japanese. No abstract available.

Cited by

• Direct observation of peptide hydrogel self-assembly.

  Adams ZC, Olson EJ, Lopez-Silva TL, Lian Z, Kim AY, Holcomb M, Zimmermann J, Adhikary R, Dawson PE. Adams ZC, et al. Chem Sci. 2022 Aug 16;13(34):10020-10028. doi: 10.1039/d1sc06562a. eCollection 2022 Aug 31. Chem Sci. 2022. PMID: 36128231 Free PMC article.

• Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis.

  Ghimire H, Garlapati C, Janssen EAM, Krishnamurti U, Qin G, Aneja R, Perera AGU. Ghimire H, et al. Cancers (Basel). 2020 Jun 27;12(7):1708. doi: 10.3390/cancers12071708. Cancers (Basel). 2020. PMID: 32605072 Free PMC article.

• Analysis of variance in spectroscopic imaging data from human tissues.

  Kwak JT, Reddy R, Sinha S, Bhargava R. Kwak JT, et al. Anal Chem. 2012 Jan 17;84(2):1063-9. doi: 10.1021/ac2026496. Epub 2011 Dec 28. Anal Chem. 2012. PMID: 22148458 Free PMC article.

• Biomolecular infrared spectroscopy: making time for dynamics.

  Hunt NT. Hunt NT. Chem Sci. 2023 Nov 28;15(2):414-430. doi: 10.1039/d3sc05223k. eCollection 2024 Jan 3. Chem Sci. 2023. PMID: 38179520 Free PMC article. Review.

• Multimodal microscopy for automated histologic analysis of prostate cancer.

  Kwak JT, Hewitt SM, Sinha S, Bhargava R. Kwak JT, et al. BMC Cancer. 2011 Feb 9;11:62. doi: 10.1186/1471-2407-11-62. BMC Cancer. 2011. PMID: 21303560 Free PMC article.

Publication types

MeSH terms

Substances