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-alpha CH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel beta-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Carver JA,Cooke RM,Esposito G,Campbell ID,Gregory H,Sheard B

doi

10.1016/0014-5793(86)80869-9

subject

Has Abstract

pub_date

1986-09-01 00:00:00

pages

77-81

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80869-9

journal_volume

205

pub_type

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