Conformational preference of Leu side chain in melanostatin in DMSO.
Indian J Biochem Biophys
;
1990 Apr; 27(2): 69-75
Article
in English
| IMSEAR
| ID: sea-28021
ABSTRACT
The solution conformation of melanostatin (Pro-Leu-Gly-NH2) in the neutral and protonated forms of DMSO has been monitored by one and two dimensional NMR techniques at 500 MHz. The temperature coefficients of the amide proton chemical shifts in conjunction with the observed NOESY spectra suggest that melanostatin in neutral form in DMSO adopts a backbone conformation such that leucine amide proton is buried by the proline ring and the side chain of leucine. Similar observation is made for protonated form of melanostatin in DMSO. The results of the present study are at variance with the earlier NMR studies which proposed a beta-turn structure for both the forms of melanostatin. There is, however, no evidence for the presence of beta-turn structure for both the forms of melanostatin in DMSO. In CDCl3 also Leu NH appears to be buried as evident from the solvent titration with DMSO and NOESY spectra.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Protein Conformation
/
Solvents
/
MSH Release-Inhibiting Hormone
/
Magnetic Resonance Spectroscopy
/
Dimethyl Sulfoxide
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1990
Type:
Article
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