TERTIARY PROTEIN STRUCTURES
\tˈɜːʃjəɹɪ pɹˈə͡ʊtiːn stɹˈʌkt͡ʃəz], \tˈɜːʃjəɹɪ pɹˈəʊtiːn stɹˈʌktʃəz], \t_ˈɜː_ʃ_j_ə_ɹ_ɪ p_ɹ_ˈəʊ_t_iː_n s_t_ɹ_ˈʌ_k_tʃ_ə_z]\
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The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
By DataStellar Co., Ltd