Applied Spectroscopy

An International Journal of Spectroscopy

A journal of the Society for Applied Spectroscopy—over 70 years of scientific excellence and education

 

Cover of Applied Spectroscopy Journal

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Complete List of Issues and Abstracts (1951 to present)

Applied Spectroscopy is one of the world's leading spectroscopy journals, publishing high-quality articles, both fundamental and applied, covering all aspects of spectroscopy. Established in 1951, the journal is owned by the Society for Applied Spectroscopy and is published monthly. The journal is dedicated to fulfilling the mission of the Society to “…advance and disseminate knowledge and information concerning the art and science of spectroscopy and other allied sciences.”  All manuscripts are rigorously peer-reviewed.

 

The journal publishes high-impact reviews, original research papers, and technical notes. In keeping with the Society's educational mandate, Focal Point Review papers are free to view. This means that the articles are freely available at the time of publication to scientists, students, and the general public worldwide.

 

With an Impact Factor (IF) of 2.087, Applied Spectroscopy is in the top quartile of journals in the Instruments and Instrumentation category and in the top half of the Spectroscopy category.

Click here for further information on Applied Spectroscopy's Aims and Scope and manuscript submission guidelines.

 


Journal Highlights

Focal Point Reviews

As noted above, the journal publishes high-impact reviews, original research papers, and technical notes. In keeping with the Society's educational mandate, Focal Point Review papers are free to view.

May 2021 Focal Point Review

Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis

 

 

 

“Can I see your passport please?”  Regulating and protecting cells at their border.    

 

 

May 2021 Focal Point Review, “Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis“

 

I live 50 km from the US-Canada border.  Before COVID, 300,000 people a day crossed the border between the USA and Canada.  Every one of those people were stopped at the border to be interrogated by an immigration/customs agent.  Their purpose is to check permits and to allow the flow of “allowable” people and goods and to prevent the movement of “undesired” people and illicit goods between the two countries.

 

Like the borders between countries, the boundary between the inside and outside of the cells of our bodies acts as a barrier that both facilitates AND prevents movement of material back and forth across it.  The immigration/customs agents are membrane proteins that sit at the border and decide on what goods can pass across and what is denied. 

 

These membrane proteins represent over a third of all the proteins in our bodies and are targets for a large number of therapeutic drugs.  Membrane receptor proteins bind to external ligands causing a conformational change that allow the movement of ions (e.g. Ca+) small molecules (glucose, amino acids) and proteins that are vital for the functioning of the cell, and our bodies, through the membrane.  Membrane proteins can also act as binding sites that are used by viruses to invade cells. For example, the deadly COVID-19 virus that has plagued the world for the past year, gains entry to cells through its’ spike-protein that binds to a membrane receptor protein called ACE-2 [See:  Front. Cell. Infect. Microbiol., 05 June 2020 | https://doi.org/10.3389/fcimb.2020.00317].  The virus gains entry using a “fake” passport.   The study of membrane proteins is critical for better understanding how viruses infect cells and how drugs can be designed to prevent them from doing so.

 

“The powerful ability to discriminate subpopulations with different FRET efficiencies and to display the time trajectories of dynamic events has made it an elegant tool to analyze biomacromolecule structures.”

 

In the feature article in the May 2021 issue of Applied Spectroscopy, “Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis“ (https://journals.sagepub.com/doi/full/10.1177/00037028211009973) ,  Meiping Zhao and members of her group in the College of Chemistry and Molecular Engineering at Peking University, review how one can better understand the details of the cells immigration/customs agents using state-of-the-art spectroscopic methods like fluorescence correlation spectroscopy (FCS) and single-molecule fluorescence resonance energy transfer (smFRET).  These methods are used to study the dynamics of conformational change, the movements, in membrane proteins.

 

Professor Zhao is a full professor at Peking University.  She has served as an Associate Editor for Applied Spectroscopy and is currently on the Editorial Advisory Board. 

 

She and her group also published a Focal Point review on “Nucleic Acid Fluorescent Probes for Biological Sensing” in Applied Spectroscopy in 2012 [Appl. Spectrosc. 2012 Nov;66(11):1249-62. doi: 10.1366/12-06803.].

 

May 5th, 2021 - Michael Blades


 

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