Cooke R M, Tappin M J, Campbell I D, Kohda D, Miyake T, Fuwa T, Miyazawa T, Inagaki F
Department of Biochemistry, University of Oxford, UK.
Eur J Biochem. 1990 Nov 13;193(3):807-15. doi: 10.1111/j.1432-1033.1990.tb19404.x.
The 1H-NMR spectra of native human epidermal growth factor (EGF) and a derivative lacking the final five residues have been assigned by two-dimensional methods, enabling their structures to be compared. The same structural features are observed for each protein, although the final five residues of native human EGF interact with residues earlier in the sequence. Comparison of the resonance shifts of human, rat and mouse EGF and human transforming growth factor alpha (TGF alpha) enables shifts characteristic of the EGF conformation to be identified, providing standards by which the structures of related proteins may be assessed.
通过二维方法已对天然人表皮生长因子（EGF）和缺少最后五个残基的衍生物的¹H-NMR光谱进行了归属，从而能够比较它们的结构。尽管天然人EGF的最后五个残基与序列中较早的残基相互作用，但每种蛋白质都观察到相同的结构特征。对人、大鼠和小鼠EGF以及人转化生长因子α（TGFα）的共振位移进行比较，能够识别出EGF构象的特征性位移，从而提供了可据此评估相关蛋白质结构的标准。
