Epidermal growth factor from the mouse. Physical evidence for a tiered .beta.-sheet domain: two-dimensional NMR correlated spectroscopy and nuclear overhauser experiments on backbone amide protons

Biochemistry ◽  
1985 ◽  
Vol 24 (14) ◽  
pp. 3783-3794 ◽  
Author(s):  
K. H. Mayo
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Two Dimensional ◽  
Beta Sheet ◽  
Physical Evidence ◽  
Backbone Amide ◽  
Epidermal Growth ◽  
Nuclear Overhauser ◽  
Amide Protons

Tertiary Structure of Mouse Epidermal Growth Factor Determined by Two-Dimensional 1H NMR

1988 ◽  
Vol 103 (5) ◽  
pp. 741-743 ◽  
Author(s):  
Daisuke Kohda ◽  
Nobuhiro Go ◽  
Kyozo Hayashi ◽  
Fuyuhiko Inagaki
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
1H Nmr ◽  
Tertiary Structure ◽  
Two Dimensional ◽  
Epidermal Growth

scholarly journals Structural characterization and exposure of aromatic residues in epidermal growth factor from the rat

1986 ◽  
Vol 239 (1) ◽  
pp. 13-18 ◽  
Author(s):  
K H Mayo ◽  
P Schaudies ◽  
C R Savage ◽  
A De Marco ◽  
R Kaptein
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Structural Domain ◽  
Solvent Exposure ◽  
Ph Titration ◽  
Aromatic Residues ◽  
Tyrosine Residues ◽  
Titration Data ◽  
Epidermal Growth ◽  
Nuclear Overhauser

Aromatic amino acid residues in epidermal growth factor (EGF) isolated from the rat have been investigated by proton n.m.r. and nuclear Overhauser methods at 500 MHz and by photochemically induced dynamic nuclear polarization (photo-c.i.d.n.p.) experiments at 360 MHz. Rat EGF contains six aromatic residues, i.e. one histidine and five tyrosine residues. pH titration data allow identification of the histidine imidazole ring protons, whereas two-dimensional n.m.r. correlated spectroscopy establishes connectivities between tyrosine ring (2,6) and (3,5) proton resonances. Photo-c.i.d.n.p. data give evidence for solvent exposure of the one histidine and the five tyrosine residues in rat EGF. Nuclear Overhauser experiments and pH titration data suggest proximity relationships among four of the tyrosine residues and the histidine residue. These data indicate the presence of a clustered, aromatic, structural domain on the protein surface and may provide a clue to the understanding of the functional structure of EGF.

scholarly journals Sequence-specific 1H-n.m.r. assignments and peptide backbone conformation in rat epidermal growth factor

1989 ◽  
Vol 257 (1) ◽  
pp. 197-205 ◽  
Author(s):  
K H Mayo ◽  
R C Cavalli ◽  
A R Peters ◽  
R Boelens ◽  
R Kaptein
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Resonance Assignments ◽  
Structural Features ◽  
Terminal Segment ◽  
Beta Sheet ◽  
Peptide Backbone ◽  
Epidermal Growth ◽  
Chain Reversal ◽  
A Chain

The solution conformation of rat epidermal growth factor (EGF) has been investigated by proton n.m.r. techniques. Two-dimensional proton n.m.r. experiments have allowed sequential resonance assignments to be made for most protons. On the basis of these assignments, two regions of anti-parallel beta-sheet structure have been derived from the n.m.r. data. A beta-sheet segment running from about V19 to V23 (capital letters refer to amino acids in the single-letter notation) is folded onto a beta-sheet segment running from R28 to N32 and joined by a chain reversal from E24 to D27. A second region involves a beta-turn from V34 to Y37, which starts a short beta-sheet up to G39, followed by a chain reversal up to Q43, which leads to folding of the C-terminal beta-sheet segment, i.e. H44-R45, running antiparallel to the short Y37 beta-sheet segment. The N-terminal segment up to G18 exists in a multiple bend conformation and is folded on to the V29-V23/R28-N32 beta-sheet such that Y10, Y13, Y22 and Y29 are proximal to each other. Structural comparison of rat, murine and human EGFs indicates a number of highly conserved structural features common to at least these species of EGF.

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