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Proton Nuclear Magnetic Resonance Study on the Solution Conformation of Human Epidermal Growth Factor
Keisuke Makino, Minoru Morimoto, Masatoshi Nishi, Shunji Sakamoto, Atsuo Tamura, Hiroshi Inooka and Kazuyuki Akasaka
Proceedings of the National Academy of Sciences of the United States of America
Vol. 84, No. 22 (Nov. 15, 1987), pp. 7841-7845
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30556
Page Count: 5
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This paper describes elucidation of the conformation of the human epidermal growth factor (hEGF) in an aqueous environment, using one- and two-dimensional proton nuclear magnetic resonance methods. The noted structural information obtained is that a rigid core structure is formed by the interplay of the three disulfide bridges and an antiparallel β -sheet consisting of Val-19 to Glu-24 and Asp-27 to Asn-32. Furthermore, the hydrophobic amino acid residues of the long C-terminal segment fold back to interact locally with residues in the β -sheet. It is suggested that the C-terminal residues play an inevitable role in the formation of the receptor-binding site.
Proceedings of the National Academy of Sciences of the United States of America © 1987 National Academy of Sciences