Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment.

Abstract:

:The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of 24 L-chain subunits, in acidic solution was studied. Using two rLF mutants, lacking four (Fer4) or eight (Fer8) N-terminal amino acid residues, the effect of N-terminal residues on the protein's stability was investigated. Of the two mutants and wild-type rLF, the tertiary and secondary structures of Fer8 were found to be most sensitive to an acidic environment. The Fer8 protein dissociated easily into subunit dimers at or below pH 2.0. Comparing the crystal structures of the mutant proteins, deletion of the N-terminal residues was found to result in fewer inter- and intra-subunit hydrogen bonds. The loss of these bonds is assumed to be responsible for lower endurance against acidic denaturation in N-terminus-deleted mutants. These results indicated that the inter- and intra-subunit hydrogen bonds of N-terminal residues affect the denaturation, especially oligomer formation of apoferritin subunits and will be of use in designing ferritin-based nanodevices.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Yoshizawa K,Mishima Y,Park SY,Heddle JG,Tame JR,Iwahori K,Kobayashi M,Yamashita I

doi

10.1093/jb/mvm187

subject

Has Abstract

pub_date

2007-12-01 00:00:00

pages

707-13

issue

6

eissn

0021-924X

issn

1756-2651

pii

mvm187

journal_volume

142

pub_type

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