Kohda D, Kodama C, Kase R, Nomoto H, Hayashi K, Inagaki F
Department of Molecular Physiology, Tokyo Metropolitan Institute of Medical Science, Japan.
Biochem Int. 1988 Apr;16(4):647-54.
The three-dimensional structure of the mouse epidermal growth factor (EGF) in solution was studied by comparison of the 1H NMR spectra of alpha EGF (1-53) and beta EGF (2-53, des-asparaginyl 1 form). Using pH dependence of chemical shifts and a two-dimensional difference spectrum, the effect of the N-terminal deletion was investigated based on the complete assignment of the proton resonances. The affected residues were all found to be located exactly in the triple-stranded, beta-sheet core in the N-terminal domain of the EGF molecule.
通过比较α-表皮生长因子（1-53）和β-表皮生长因子（2-53，去天冬酰胺基1形式）的1H NMR谱，研究了溶液中小鼠表皮生长因子（EGF）的三维结构。利用化学位移的pH依赖性和二维差异谱，基于质子共振的完全归属研究了N端缺失的影响。发现受影响的残基都恰好位于EGF分子N端结构域的三链β-折叠核心中。
