Journals on Biomedical Imaging - BJSTR Journal

Abstract

#Amino acids are small organic molecules having both amino and carboxylic acid groups bound to the a-carbon, with a general formula NH2- CH(R)-COOH. Their side chains, R, can vary - saml our bulky, #hidrophobic our #hydrophilic, polar, charged or neutral. If the a-carbon is bound to four different chemical groups, the amino acid is chiral and two isomers exist labeled with L our D. Furthermore, the parameters characterizing the motions of amino acids in crystal can be comparable with those describing this dynamics in #biopolymers. Therefore, possessing information on the strusture and dynamics of single amino acids is important in biochemistry, biophysics, medicine and pharmacy. The structure and dynamics of crystalline amino acids can be followed in a wide temperature and pressure range by diffraction and various spectroscopic techniques and the results can be interpreted, giving the characteristic times of selected motions and the values of related energy barriers. #L-methionine (Figure 1) is an essential amino acid important in the #methylation process playing a key role in the immune system affected by HIV [1] and other diseases (like Alzheimer and Parkinson [2]) . However very few studies crystalline L- methionine have been reported in the literature [3] thus very little is known about its #physical properties. The aim of this study is to investigate the stucture-property relations in L- methionine as a function temperature, because of according to recent experiments, including Raman spectroscopy, #thermal analysis, neutron diffraction and inelastic neutron scattering, changes in the conformational states of L-methionine induce a variety of structural arrangements between 220 and 340 K.

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Combining X-Rays and Neutrons to Shed Light in the Conformational Changes in #Aminoacids by Margareth KKD Franco in BJSTR