PROTEIN ALPHA HELICAL CONFORMATION
\pɹˈə͡ʊtiːn ˈalfə hˈɛlɪkə͡l kɒnfɔːmˈe͡ɪʃən], \pɹˈəʊtiːn ˈalfə hˈɛlɪkəl kɒnfɔːmˈeɪʃən], \p_ɹ_ˈəʊ_t_iː_n ˈa_l_f_ə h_ˈɛ_l_ɪ_k_əl k_ɒ_n_f_ɔː_m_ˈeɪ_ʃ_ə_n]\
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The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
By DataStellar Co., Ltd
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Proto Oncogene Proteins c erbB 2
- cell surface protein-tyrosine kinase that is found to be overexpressed in significant number adenocarcinomas. It has extensive homology can heterodimerize EGF EPIDERMAL GROWTH FACTOR), 3 receptor (RECEPTOR, 3) and the 4 receptor. Activation of erbB-2 receptor occurs during heterodimer formation with a ligand-bound erbB family members. EC 2.7.11.-.