Infrared spectroscopy of proteins.

This review deals with current concepts of vibrational spectroscopy for the investigation of protein structure and function. While the focus is on infrared (IR) spectroscopy, some of the general aspects also apply to Raman spectroscopy. Special emphasis is on the amide I vibration of the polypeptide backbone that is used for secondary-structure analysis. Theoretical as well as experimental aspects are covered including transition dipole coupling. Further topics are discussed, namely the absorption of amino-acid side-chains, 1H/2H exchange to study the conformational flexibility and reaction-induced difference spectroscopy for the investigation of reaction mechanisms with a focus on interpretation tools.

https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0033583502003815

What vibrations tell us about proteins

Recent advances in nanoscience and nanotechnology radically changed the way we diagnose, treat, and prevent various diseases in all aspects of human life. Silver nanoparticles (AgNPs) are one of the most vital and fascinating nanomaterials among several metallic nanoparticles that are involved in biomedical applications. AgNPs play an important role in nanoscience and nanotechnology, particularly in nanomedicine. Although several noble metals have been used for various purposes, AgNPs have been focused on potential applications in cancer diagnosis and therapy. In this review, we discuss the synthesis of AgNPs using physical, chemical, and biological methods. We also discuss the properties of AgNPs and methods for their characterization. More importantly, we extensively discuss the multifunctional bio-applications of AgNPs; for example, as antibacterial, antifungal, antiviral, anti-inflammatory, anti-angiogenic, and anti-cancer agents, and the mechanism of the anti-cancer activity of AgNPs. In addition, we discuss therapeutic approaches and challenges for cancer therapy using AgNPs. Finally, we conclude by discussing the future perspective of AgNPs.

/pdf/silver-nanoparticles-synthesis-characterization-properties-1gs52z8tm7.pdf

Silver Nanoparticles: Synthesis, Characterization, Properties, Applications, and Therapeutic Approaches

Amino acid side chains play fundamental roles in stabilising protein structures and in catalysing enzymatic reactions. These fields are increasingly investigated by infrared spectroscopy at the molecular level. To help the interpretation of the spectra, a review of the infrared absorption of amino acid side chains in H(2)O and 2H(2)O is given. The spectral region of 2600-900cm(-1) is covered.

The infrared absorption of amino acid side chains.

Robust biomacromolecules could be used for a wide range of biotechnological applications. Here the authors report a biomimetic mineralization process, in which biomolecules are encapsulated within metal-organic frameworks, and their stability is subsequently increased without significant bioactivity loss.

/pdf/biomimetic-mineralization-of-metal-organic-frameworks-as-3016mgsldz.pdf

Biomimetic mineralization of metal-organic frameworks as protective coatings for biomacromolecules.

This paper reviews state-of-the-art reaction-induced infrared difference spectroscopy of proteins. This technique enables detailed characterization of enzyme function on the level of single bonds of proteins, cofactors, or substrates. The following methods to initiate a reaction in the infrared sample are discussed: (i) light-induced difference spectroscopy, (ii) attenuated total reflection with buffer exchange, (iii) the infrared variant of stopped and continuous flow, (iv) temperature and pressure jump, (v) photolytical release of effector substances from caged compounds, (vi) equilibrium electrochemistry, and (vii) photoreduction. Illustrating applications are given including hot topics from the fields of bioenergetics, protein folding, and molecule--protein interaction.

Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms.

The invention relates to an infrared measuring device, especially for the spectrometry of aqueous systems. Said device comprises at least one measuring unit, especially a measuring cell, also comprising at least one ATR-body and at least one infrared light source. The measuring unit contains at least one ATR-body which comprises at least two planar, substantially parallel limiting surfaces and which is transparent with respect to measuring radiation and which has an index of refraction which is greater than that of the medium which is arranged next to at least one limiting surface and which is to be examined, especially larger or equal to 1.5. The IR-measuring radiation on at least one of the planar, parallel limiting surfaces of the ATR-body can be totally reflected in an attenuated manner by at least six times.

Infrared measuring device, especially for the spectrometry of aqueous systems, preferably multiple component systems

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2800%2901782-8

Christian Zscherp

Papers

What vibrations tell us about proteins

Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms.

Infrared measuring device, especially for the spectrometry of aqueous systems, preferably multiple component systems

Substrate binding and enzyme function investigated by infrared spectroscopy.

Effect of proline to alanine mutation on the thermal stability of the all-β-sheet protein tendamistat