Open AccessPreliminary assignments of the aromatic and some methyl group resonances of the 1 H‐NMR spectrum of the oxidized form of uteroglobin
Author(s) -
JAMIN Nadège,
ROY Pierre,
FRIDLANSKY Françoise,
DELEPIERRE Muriel,
MILGROM Edwin,
ROQUES Bernard P.,
MOR JeanPaul
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14916.x
Subject(s) - uteroglobin , chemistry , crystallography , crystal structure , group (periodic table) , methyl group , nuclear magnetic resonance , stereochemistry , physics , organic chemistry , biochemistry , gene
Two‐dimensional NMR methods have been used to assign aromatic and methyl group resonances in the 1 H‐NMR spectrum of oxidized uteroglobin. Assignments to specific amino acids are based on X‐ray‐determined structures of two crystal forms (C222 1 and P2 1 ) and on an energy‐minimized X‐ray structure of the C222 1 form of uteroglobin. These preliminary assignments are sufficient to probe the interaction of oxidized uteroglobin with progesterone in solution. The protein global structure is unmodified but some direct or indirect conformational changes are induced in the H 1 H 4 (H 1 ′H 4 ′) pockets and close to Phe28 by progesterone.