Physical characterization of a totally synthetic rubredoxin.

Abstract:

:The entire polypeptide of hyperthermophilic Pyrococcus furiosus rubredoxin was synthesized in order to specifically probe structural determinants of protein thermostability. The uv-visible, circular dichroic, electron paramagnetic, and nuclear magnetic resonance spectra, and electrochemical properties, of the native and synthetic proteins were essentially identical. The synthetic protein had a half-life for denaturation of 24 hr at 80 degrees C. The synthetic protein is considerably more thermostable than nonhyperthermophilic rubredoxins, but not as stable as the native protein. Based on the spectroscopic evidence, it appears that the synthetic protein is incorporating iron properly to form holoprotein, but the peptide still may not be folded correctly.

journal_name

J Inorg Biochem

authors

Christen R,Jancic T,Zhou ZH,Adams MW,Tomich JM,Smith ET

doi

10.1016/s0162-0134(96)00079-7

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

53-6

issue

1

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(96)00079-7

journal_volume

65

pub_type

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