This chapter discusses the properties of amino acids in sequences. The basic properties of the amino acid side chains can be typified by the number of atoms, the number of polar atoms that they contain and the degree to which the atoms are constrained. The most common modification of the ...
Taylor & Francis Online :: Electronic Properties of the Amino Acid Side Chains Contribute to the Structural Preferences in Protein Folding - Journal of Bio... Taylor & Francis Online :: Electronic Properties of the Amino Acid Side Chains Contribute to the Structural Preferences in Protein Folding ...
Why is it important to understand the chemical properties of amino acid side chains in order to understand protein structure and function? Briefly explain the 20 known amino acids. How do Hsp70-like proteins affect existing interactions between proteins?
nickel peptide complexesamino acid side chainsCoordination of proteins and peptides to metal ions is known to affect their properties, often by a change ... S Medici,M Peana,Nurchi, Valeria,... - 《Molecules》 被引量: 11发表: 2013年 Coordination behavior of N-benzoylamino acids: Synthesis...
LAT1 relics on the hydrophobic interaction between substrate amino acid side chains and the substrate binding site, so that many variations are possible for the substrate amino acid side chains, which is the basis of the broad substrate selectivity. System L transporters, thus, function as a ...
On one hand, amino acid side chains in the active site may act as weak acids and bases with critical functions that depend on their maintaining a certain state of ionization, and elsewhere in the protein, ionized side chains may play an essential role in the interactions that maintain protein...
Hereby, the aggregation propensity of unfolded polypeptide chains appears to be correlated to physicochemical properties like hydrophobicity, secondary structure propensity and charge [70], which can be inferred from the amino acid sequence of both the target protein and the fusion [71]. We here ...
This allows control over the spatial orientation of the amino acid side chain (α -substituent) and in turn modulation of the self-assembly of CDPs. It is important to note that the molecular weights of the CDPs utilized in the current study are only about 0.2 kDa, whereas the ...
The branched amino acids featured multiple carboxylic acids in their side chains, making the fluorescent-peptide dendrimers highly water-soluble compared with the analogous peptides containing the fluorescent amino acids only. The branched amino acid units also improved the fluorescence intensity of the ...
Furthermore, the tertiary structure of protein in conjugate changed with decreasing number of aromatic side-chains exposed in heating environment. The decrease in fluorescence intensity of conjugate was related to conformational changes due to presence of GA. Graphical abstract Download: Download high-...