A high resolution 1H NMR study of the solution structure of human epidermal growth factor

J. A. Carver; R. M. Cooke; G. Esposito; I. D. Campbell; H. Gregory; B. Sheard

doi:10.1016/0014-5793(86)80869-9

A high resolution ₁H NMR study of the solution structure of human epidermal growth factor

J. A. Carver, R. M. Cooke, G. Esposito, I. D. Campbell, H. Gregory, B. Sheard

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

500 MHz ¹H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1-48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.

Original language	English (US)
Pages (from-to)	77-81
Number of pages	5
Journal	FEBS Letters
Volume	205
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(86)80869-9
State	Published - Sep 1 1986

Keywords

(Human EGF)
Growth factor
NMR
Protein structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(86)80869-9

Cite this

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title = "A high resolution 1H NMR study of the solution structure of human epidermal growth factor",

abstract = "500 MHz 1H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1-48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.",

keywords = "(Human EGF), Growth factor, NMR, Protein structure",

author = "Carver, {J. A.} and Cooke, {R. M.} and G. Esposito and Campbell, {I. D.} and H. Gregory and B. Sheard",

note = "Funding Information: We wish to thank the MRC, the SERC and G.D. Searle for their financial support. We also thank Dr J. Boyd, M. Baron and N. Soffe for their assistance.",

year = "1986",

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T1 - A high resolution 1H NMR study of the solution structure of human epidermal growth factor

AU - Carver, J. A.

AU - Cooke, R. M.

AU - Esposito, G.

AU - Campbell, I. D.

AU - Gregory, H.

AU - Sheard, B.

N1 - Funding Information: We wish to thank the MRC, the SERC and G.D. Searle for their financial support. We also thank Dr J. Boyd, M. Baron and N. Soffe for their assistance.

PY - 1986/9/1

Y1 - 1986/9/1

N2 - 500 MHz 1H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1-48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.

AB - 500 MHz 1H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1-48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.

KW - (Human EGF)

KW - Growth factor

KW - NMR

KW - Protein structure

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