Amino acids physicochemical properties

The results of the study also indicate how contribution estimates can be used to map each individual amino acid (and each amino acid physicochemical property) in the receptors with respect to its contribution to the activity and selectivity for every amine ligand [14a],... 

Table 1. Physicochemical Properties of the Natural Amino Acids ...

A thorough discussion of the mechanisms of absorption is provided in Chapter 4. Water-soluble vitamins (B2, B12, and C) and other nutrients (e.g., monosaccharides, amino acids) are absorbed by specialized mechanisms. With the exception of a number of antimetabolites used in cancer chemotherapy, L-dopa, and certain antibiotics (e.g., aminopenicillins, aminoceph-alosporins), virtually all drugs are absorbed in humans by a passive diffusion mechanism. Passive diffusion indicates that the transfer of a compound from an aqueous phase through a membrane may be described by physicochemical laws and by the properties of the membrane. The membrane itself is passive in that it does not partake in the transfer process but acts as a simple barrier to diffusion. The driving force for diffusion across the membrane is the concentration gradient (more correctly, the activity gradient) of the compound across that membrane. This mechanism of... 

Some of the many hypotheses and models will be presented briefly. The physicochemical hypothesis refers to a minimalisation of the liability of the genetic code to cause errors in information transmission. The error rate can fall when amino acids with similar codons have similar properties, such as the presence of hydrophilic... 

A new quality in the analysis of hydrophobically post-translational modified proteins could be achieved by the construdion of lipidated proteins in a combination of bioorganic synthesis of activated lipopeptides and bacterial expression of the protein backbone as described before. The physicochemical properties of such artificial lipoproteins differ substantially from those of the corresponding lipopeptides. The pronounced dominance of the hydrophilic protein moiety (e.g. for the Ras protein 181 amino acids) over a short lipopeptide with one or two hydrophobic modifications keeps the construct soluble up to 1CT4 M, while the biotinylated or fluorescence labeled lipopeptides exhibit low solubility in aqueous solutions and can be applied in the biophysical experiments only in vesicle integrated form or dissolved in organic solvent. 

Scientists carry out searches on databases. Each EST of interest can be compared with sequences in proteins, and the degree of match can be determined. A technique called threading is used. This involves using data on three-dimensional (3D) protein structure, coupled with knowledge of the physicochemical properties of amino acids, to determine if the amino acid sequence is likely to fold in the same way as a sequence for which the structure is known. In this way, more information about the putative target protein can be assessed. 

A peptide is essentially comprised of L-amino acid residues, and the peptide backbone may be critical to provide physicochemical and functional properties. Diverse functionalities induced by peptides in natural protein hydrolysates are being received with much interest in food industries or alternative-medicinal food sciences. The latest year s researches... 

N-Acetylalanyl N -methylamide, 2ll3f Aclacinomycin A, 8i1,87f Acridine orange intercalator, 125f Adrenocorticotropic hormone (ACTH) D-amino acids and activity, 155-58 biological and physicochemical properties, 158-62 chain length and... 

Bioactive sequences of up to six amino acid residues known to assume (1- or "/-turns in the bioactive conformation are suitable for such libraries. If the sequence is short, residues have to be added in a manner to retain the desired physicochemical properties of the peptide (e.g., to short polar active sequences hydrophobic residues are preferentially added and vice versa). The choice of the scaffold depends on the number of structure-inducing amino acids such as Gly or Pro present in the native sequence. In absence of such residues scaffolds (1) or (4) (Scheme 24) are selected, whereas if Gly or Pro is present alternative scaffolds can be considered. Then the components of the four stereoisomeric sublibraries of Scheme 26 (or their equivalents if other scaffolds are chosen) are synthesized according to procedures described in the preceding sections. 

Klein et al. (1986) reported the compositional or physicochemical properties (attributes) of amino acid sequences in 1603 protein sequences to establish a classification system for 26 protein functions. These results showed that three or four attributes were generally sufficient to distinguish each of the 26 functional categories from the remainder of the database. The attributes used were related to hydrophobicity, charge and its distribution (frequency or... 

Separation of diastereoisomeric peptides by HPLC is more common. Since each diastereo-isomer has different physicochemical and biological properties, this is of great interest. Separations of diastereoiosomeric di- and tripeptides have usually been performed on reversed-phase columns. Cahill et al. (119) separated diastereoisomeric amino acids and derivatized dipeptides using esters of the /V-hydroxysuccinamide of f-butyl carbonyl-L-amino acid on Cl8 and C8 columns. Linder et al. (120) separated amino acid and peptide derivatives on an RP-C8 column, adding a metal chelate. Mixtures of DL and LD-dipeptides can be separated by RP-HPLC into two peaks, one containing LL- and DD-isomers, the other containing LD and DL-isomers. Sep-... 

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