Oxidative Folding of Peptides and Proteins

2008 ◽  
Keyword(s):  
Oxidative Folding

Oxidative Folding of the Cystine Knot Motif in Cyclotide Proteins

2005 ◽  
Vol 12 (2) ◽  
pp. 147-152 ◽  
Author(s):  
David Craik ◽  
Norelle Daly
Keyword(s):  
Oxidative Folding ◽  
Cystine Knot

scholarly journals The Mitochondrial Intermembrane Space Oxireductase Mia40 Funnels the Oxidative Folding Pathway of the CytochromecOxidase Assembly Protein Cox19

2014 ◽  
Vol 289 (14) ◽  
pp. 9852-9864 ◽  
Author(s):  
Hugo Fraga ◽  
Joan-Josep Bech-Serra ◽  
Francesc Canals ◽  
Gabriel Ortega ◽  
Oscar Millet ◽  
...  
Keyword(s):  
Folding Pathway ◽  
Intermembrane Space ◽  
Oxidative Folding ◽  
Mitochondrial Intermembrane Space

Oxidative folding of ω-conotoxin MVIIC: Effects of temperature and salt

Biopolymers ◽  
1996 ◽  
Vol 38 (6) ◽  
pp. 733-744 ◽  
Author(s):  
Shigeru Kubo ◽  
Naoyoshi Chino ◽  
Terutoshi Kimura ◽  
Shumpei Sakakibara
Keyword(s):  
Oxidative Folding ◽  
Effects Of Temperature

scholarly journals Interlocking Disulfides in Circular Proteins: Toward Efficient Oxidative Folding of Cyclotides

2011 ◽  
Vol 14 (1) ◽  
pp. 77-86 ◽  
Author(s):  
Teshome Leta Aboye ◽  
Richard J. Clark ◽  
Robert Burman ◽  
Marta Bajona Roig ◽  
David J. Craik ◽  
...  
Keyword(s):  
Oxidative Folding ◽  
Circular Proteins

scholarly journals Two new structured intermediates in the oxidative folding of RNase A

FEBS Letters ◽  
1999 ◽  
Vol 460 (3) ◽  
pp. 477-479 ◽  
Author(s):  
Ervin Welker ◽  
Mahesh Narayan ◽  
Michael J Volles ◽  
Harold A Scheraga
Keyword(s):  
Rnase A ◽  
Oxidative Folding

scholarly journals Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes

2015 ◽  
Vol 4 (11) ◽  
pp. 758-770 ◽  
Author(s):  
Mark P. Jedrychowski ◽  
Libin Liu ◽  
Collette J. Laflamme ◽  
Kalypso Karastergiou ◽  
Tova Meshulam ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Oxidative Folding ◽  
Upstream Regulator

The Oxidative Folding and Misfolding of Human Leukocyte Antigen-B27

2011 ◽  
Vol 15 (3) ◽  
pp. 669-684 ◽  
Author(s):  
Antony N. Antoniou ◽  
David B. Guiliano ◽  
Izabela Lenart ◽  
Garth Burn ◽  
Simon J. Powis
Keyword(s):  
Human Leukocyte Antigen ◽  
Human Leukocyte ◽  
Oxidative Folding ◽  
Leukocyte Antigen

scholarly journals Mutations in the B-domain of insulin-like growth factor-I influence the oxidative folding to yield products with modified biological properties

1995 ◽  
Vol 308 (3) ◽  
pp. 865-871 ◽  
Author(s):  
S J Milner ◽  
G L Francis ◽  
J C Wallace ◽  
B A Magee ◽  
F J Ballard
Keyword(s):  
Growth Factor ◽  
Biological Properties ◽  
Insulin Like Growth Factor ◽  
Igf Binding Proteins ◽  
Oxidative Folding ◽  
Biological Assays ◽  
Igf I ◽  
Igf Binding ◽  
L6 Myoblast

The oxidative folding of human insulin-like growth factor (IGF)-I yields two major disulphide folding isomers. In the present study, B-domain analogues of IGF-I were used to investigate the effect of mutations on the folding reaction and to investigate the functional implications of misfolding. The analogues used were substitutions of the native Glu3 by Gly or Arg, or the native Glu9 by Lys. IGF-I and these analogues were also prepared attached to a hydrophobic 13-amino-acid N-terminal extension, Met-Phe-Pro-Ala-Met-Pro-Leu-Ser-Ser-Leu-Phe-Val-Asn, referred to as ‘Long-IGF-I’ analogues. Each IGF was fully reduced and refolded to yield native and misfolded isomers, which were subsequently purified for biological characterization. Analysis of the folding reaction at equilibrium revealed a distribution of folding isomers characteristic for each peptide. The yield of the native disulphide folding isomer was increased for the Glu3 substitutions, but not for the Glu9 substitution. The main alternative folding isomer was present in the IGF-I analogues in reduced proportions. Except for [Gly3]IGF-I the N-terminal extension increased the yield of the native isomer which was maximal for the analogue Long-[Arg3]IGF-I. A folding intermediate for the latter analogue was isolated and partially characterized. The biological assays showed that all the main alternative isomers bound poorly to IGF-binding proteins (IGFBPs) secreted by L6 myoblasts. Moreover, these isomers bound to the type 1 IGF receptor with 0.5-25% the affinity of the native isomer. In a rat L6 myoblast protein-synthesis assay, the observed biological activity of the native and main alternative isomers was explained by their modified IGFBP- and receptor-binding properties. We propose that the N-terminal extension imparts a steric constraint at a crucial point in folding, thus allowing native disulphide bonds to form efficiently.

scholarly journals The MIA pathway: A tight bond between protein transport and oxidative folding in mitochondria

2012 ◽  
Vol 1823 (7) ◽  
pp. 1142-1150 ◽  
Author(s):  
Diana Stojanovski ◽  
Piotr Bragoszewski ◽  
Agnieszka Chacinska
Keyword(s):  
Protein Transport ◽  
Oxidative Folding
Sign in / Sign up

Export Citation Format

Share Document