Solution Structure of Apo Cu,Zn Superoxide Dismutase:  Role of Metal Ions in Protein Folding†

Biochemistry ◽  
2003 ◽  
Vol 42 (32) ◽  
pp. 9543-9553 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Fiorenza Cramaro ◽  
Rebecca Del Conte ◽  
Maria Silvia Viezzoli
Keyword(s):  
Superoxide Dismutase ◽  
Protein Folding ◽  
Metal Ions ◽  
Solution Structure

Superoxide Dismutase Folding/Unfolding Pathway: Role of the Metal Ions in Modulating Structural and Dynamical Features

2003 ◽  
Vol 330 (1) ◽  
pp. 145-158 ◽  
Author(s):  
Michael Assfalg ◽  
Lucia Banci ◽  
Ivano Bertini ◽  
Paola Turano ◽  
Paul R. Vasos
Keyword(s):  
Superoxide Dismutase ◽  
Metal Ions ◽  
Dynamical Features

Adaptive Role of Lipids in Algae under Metal Ions Impact (a Review)

2018 ◽  
Vol 54 (6) ◽  
pp. 78-93
Author(s):  
V. V. Grubinko ◽  
O. I. Bodnar ◽  
A. I. Lutsiv ◽  
G. B. Viniarska
Keyword(s):  
Metal Ions ◽  
Adaptive Role

scholarly journals The Role of the Disulfide Bridge in the Copper (II) Binding by the Cyclic His4-Peptide

2021 ◽  
Vol 22 (12) ◽  
pp. 6458
Author(s):  
Aleksandra Pieniężna ◽  
Weronika Witak ◽  
Aneta Szymańska ◽  
Justyna Brasuń
Keyword(s):  
Metal Ions ◽  
Coordination Mode ◽  
Transition Metal Ions ◽  
Disulfide Bridge ◽  
Chain Flexibility ◽  
Vis Spectroscopy ◽  
Ph Range ◽  
Cd Studies ◽  
Metal Ratios

In this paper, we present studies on the influence of the disulfide bridge on the copper (II) ions’ binding abilities by the cyclic His4-peptide. The studied ligand HKHPHRHC-S-S-C consists of nine amino acids. The cyclic structure was obtained through a disulfide bridge between two cysteinyl groups. Moreover, this peptide is characterized by the presence of four His residues in the sequence, which makes it an interesting ligand for transition metal ions. The potentiometric and spectroscopic (UV-Vis spectroscopy and circular dichroism spectroscopy (CD)) studies were carried out in various molar ligand to metal ratios: 2:1, 1:1, and 1:2, in the pH range of 2.5–11 at 25 °C. The results showed that the cyclic His4-peptide promotes dinuclear complexes in each of these systems and forms the final dinuclear species with the {NIm, 3N-amide}{NIm, 3N-amide} coordination mode. The obtained data shows that cyclization by the formation of the disulfide bond has an impact on the peptide chain flexibility and appearance of additional potential donors for metal ions and influences the copper (II) ions’ coordination.

Folding of peptides and proteins: role of disulfide bonds, recent developments

2013 ◽  
Vol 4 (6) ◽  
pp. 597-604 ◽  
Author(s):  
Yuji Hidaka ◽  
Shigeru Shimamoto
Keyword(s):  
Protein Folding ◽  
Disulfide Bonds ◽  
Bond Formation ◽  
Difficult Problem ◽  
Chemical Methods ◽  
Mutant Proteins ◽  
Folding Intermediates ◽  
Peptide Chemistry ◽  
Recent Developments

AbstractDisulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction. However, regulating or analyzing the structures of folding intermediates of peptides and proteins continues to be a difficult problem. Recently, the development of several techniques in peptide chemistry and biotechnology has resulted in the availability of some powerful tools for studying protein folding in the context of the structural analysis of native, mutant proteins, and folding intermediates. In this review, recent developments in the field of disulfide-coupled peptide and protein folding are discussed, from the viewpoint of chemical and biotechnological methods, such as analytical methods for the detection of disulfide pairings, chemical methods for disulfide bond formation between the defined Cys residues, and applications of diselenide bonds for the regulation of disulfide-coupled peptide and protein folding.

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