Near-infrared spectroscopy and imaging in protein research

Abstract Protein research by near-infrared (NIR) spectroscopy stretches back more than 25 years, however, it has not been well established yet. One of the most difficult parts comes from the fact that the key bands for investigating protein secondary structure are the combination bands such as those due to a combination of N–H stretching vibration and amide II modes. This review provides some explanation of how one can correlate the combination modes with protein secondary structure using several examples. One of the most important advantages of NIR protein research is that one can explore a change in hydration as well as that in the protein secondary structure at the same time. It is rather difficult for IR and Raman spectroscopy to investigate them simultaneously. In this review, we outline characteristic features of NIR spectroscopy in protein research first, and then band assignments of NIR spectra of proteins are described. After that several examples of NIR studies of proteins are introduced. Finally, as examples of NIR imaging to protein research, recent studies on fish egg development are discussed.

• Publication year

  2020

• Venue

  Unknown venue

• Publication date

  Unknown publication date

• Fields of study

  Biology, Materials Science, Chemistry

• Identifiers
  DOI 10.1016/b978-0-12-818610-7.00006-2
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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