One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c.

Abstract:

:The effect of S-methylating cysteine-102 (cys-102) (SH----SSCH3) of yeast isozyme-1 (iso-1) ferricytochrome c has been studied using proton NMR spectroscopy. COSY, NOESY, and one-dimensional nuclear Overhauser effect (NOE) difference spectroscopies have all been used. The NMR spectrum of this derivative is very similar to that of native yeast iso-1 ferricytochrome c. The advantage of using the cys-102 S-methylated derivative is that it is unable to spontaneously dimerize in solution, like native iso-1 monomer does. This makes the derivative a simple, ideal protein for long NMR experiments. This work yields many proton resonance assignments for S-methylated yeast iso-1 monomer and confirms all of the assignments for iso-1 monomer that were previously made using only the one-dimensional NOE method.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Busse SC,Moench SJ,Satterlee JD

doi

10.1016/S0006-3495(90)82352-3

subject

Has Abstract

pub_date

1990-07-01 00:00:00

pages

45-51

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(90)82352-3

journal_volume

58

pub_type

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