Chiral molecules proteins

Because proteins are made up of L-amino acids, they exhibit chirality in their structures, lacking planes or points of symmetry. Proteins also can exhibit chirality in their interactions with other chiral molecules as well as prochiral centers in other molecules. This latter point is beautifully illustrated by fumarase s catalysis of the dehydration of L-malate, a molecule containing two seemingly equivalent hydrogen atoms ... 

Stereoselective catalysis using biocatalysts (e.g. enzymes) and also of rationally designed small chiral molecules, deals essentially with the same principle the spatial and selective docking of guest molecules to a chiral host molecule to form complementary interactions to form reversible transient molecule associates (see the specific sections in this volume). The enantiomeric excess of a certain reaction and hence the result will be determined by the degree of chiral discrimination. Along the same theoretical lines the concepts of protein (enzyme, antibody, etc.) mimicks via imprinted" synthetic polymers should be mentioned and will be discussed further. 

Chirality Many objects around us are handed. For example, our left and right hands are mirror images of each other, and caimot be superimposed on each other. Other chiral objects include shoes, gloves and printed pages. Many molecules are also handed, i.e. they cannot be superimposed on their mirror images. Such molecules are called chiral molecules. Many compounds that occur in living organisms, e.g. carbohydrates and proteins, are chiral... 

In living organisms, chiral molecules are usually present in only one of their chiral forms. For example, the amino acids in proteins occur only as their l isomers glucose occurs only as its D isomer. (The conventions for naming stereoisomers of the amino acids are described in Chapter 3 those for sugars, in Chapter 7 the RS system, described above, is the most useful for some biomolecules.) In contrast, when a compound with an asymmetric carbon atom is chemically synthesized in the laboratory, the reaction usually pro-... 

The most popular and commonly used chiral stationary phases (CSPs) are polysaccharides, cyclodextrins, macrocyclic glycopeptide antibiotics, Pirkle types, proteins, ligand exchangers, and crown ether based. The art of the chiral resolution on these CSPs has been discussed in detail in Chapters 2-8, respectively. Apart from these CSPs, the chiral resolutions of some racemic compounds have also been reported on other CSPs containing different chiral molecules and polymers. These other types of CSP are based on the use of chiral molecules such as alkaloids, amides, amines, acids, and synthetic polymers. These CSPs have proved to be very useful for the chiral resolutions due to some specific requirements. Moreover, the chiral resolution can be predicted on the CSPs obtained by the molecular imprinted techniques. The chiral resolution on these miscellaneous CSPs using liquid chromatography is discussed in this chapter. 

Abstract Now an incisive probe of biomolecular structure, Raman optical activity (ROA) measures a small difference in Raman scattering from chiral molecules in right- and left-circularly polarized light. As ROA spectra measure vibrational optical activity, they contain highly informative band structures sensitive to the secondary and tertiary structures of proteins, nucleic acids, viruses and carbohydrates as well as the absolute configurations of small molecules. In this review we present a survey of recent studies on biomolecular structure and dynamics using ROA and also a discussion of future applications of this powerful new technique in biomedical research. 

Whereas conventional products are often achiral organic molecules or polymers, the product range of biotechnological processes often encompasses chiral molecules or biopolymers such as proteins, nucleic acids, or carbohydrates. 

Contrary to conventional HPLC, almost 98% of chiral resolution in CE is carried out using the chiral selector as a mobile phase additive. Again all the common chiral selectors used in NLC can also be used in NCE. But, unfortunately, few chiral molecules have been tested in NCE for enantiomeric resolution of some racemates. To the best of our knowledge only cyclodextrins and protein-based chiral mobile phase additives have been used for this purpose. Manz and coworkers discussed chiral separations by NCE in their reviews in 2004 [21] and 2006 [22], Later on, Pumera [16] reviewed the use of microfluidic devices for enantiomeric resolutions in capillary electrophoresis. Not much work has been carried out on chiral resolution in NCE but the papers that are available are discussed here. 

Except for the property of rotating plane-polarized light in opposite directions, the physical properties of enantiomers of the same compound are identical. In addition, their chemical properties are identical, except when they are acted upon by another chiral molecule. One such kind of molecule consists of enzymes, large molecules of proteins that catalyze biochemical reactions. Therefore, many biochemical reactions involve chiral molecules. 

Besides the continuous improvements of FTIR-VCD instruments described above, some exciting new developments related to VCD measurements have been reported in recent years. These include the developments of matrix isolation FTIR-VCD instruments and of laser based real time VCD spectrometers. These new developments are associated with brand new applications and research directions, such as combining the matrix isolation technique with VCD spectroscopy to probe conformationally flexible chiral molecules and H-bonded chiral molecular complexes, and using femtosecond laser VCD instruments to record time resolved VCD spectra for monitoring fast chemical reactions or folding and unfolding events of peptides and proteins in solution. These will be discussed in more detail in Sects. 4.5 and 4.6. 

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