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deciphering protein–protein interactions. part i. experimental techniques and databases破译蛋白质相互作用。.pdf

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deciphering protein–protein interactions. part i. experimental techniques and databases破译蛋白质相互作用。

Education Deciphering Protein–Protein Interactions. Part I. Experimental Techniques and Databases * Benjamin A. Shoemaker, Anna R. Panchenko amino acids are preferred on protein interfaces and that the amino acid composition of the core differs considerably from the rim [6,7,9,10]. More recent models suggested that the protein binding site consists of a few independent highly packed regions, so called ‘‘hot spots,’’ which contribute signiﬁcantly to the free energy of binding [11–13]. Hot spots were found to be structurally conserved [14], and the energetics of interactions at the hot spots have been analyzed in several studies [15–18]. In many cellular processes, proteins recognize speciﬁc roteins interact with each other in a highly speciﬁc targets and bind them in a highly regular manner. The Pmanner, and protein interactions play a key role in speciﬁcity of interactions in these cases is determined by many cellular processes; in particular, the distortion structural and physico–chemical properties of two of protein interfaces may lead to