Solution structure of S-DNA formed by covalent base pairing involving a disulfide bond

2012 ◽  
Vol 10 (36) ◽  
pp. 7327 ◽  
Author(s):  
Akihiko Hatano ◽  
Munehiro Okada ◽  
Gota Kawai
Keyword(s):  
Disulfide Bond ◽  
Solution Structure ◽  
Base Pairing

scholarly journals NMR Solution Structure of the Integral Membrane Enzyme DsbB: Functional Insights into DsbB-Catalyzed Disulfide Bond Formation

2008 ◽  
Vol 31 (6) ◽  
pp. 896-908 ◽  
Author(s):  
Yunpeng Zhou ◽  
Tomasz Cierpicki ◽  
Ricardo H. Flores Jimenez ◽  
Stephen M. Lukasik ◽  
Jeffrey F. Ellena ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Solution Structure ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Nmr Solution Structure ◽  
Membrane Enzyme

The Single Disulfide-Directed β-Hairpin Fold: Role of Disulfide Bond in Folding and Effect of an Additional Disulfide Bond on Stability

2020 ◽  
Vol 73 (4) ◽  
pp. 312
Author(s):  
Balasubramanyam Chittoor ◽  
Bankala Krishnarjuna ◽  
Rodrigo A. V. Morales ◽  
Raymond S. Norton
Keyword(s):  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Solution Structure ◽  
Conformational Stability ◽  
Disulfide Bridge ◽  
Solution Nmr ◽  
Peptide Epitope ◽  
The Core ◽  
Native Fold

Disulfide bonds play a key role in the oxidative folding, conformational stability, and functional activity of many peptides. A few disulfide-rich peptides with privileged architecture such as the inhibitor cystine knot motif have garnered attention as templates in drug design. The single disulfide-directed β-hairpin (SDH), a novel fold identified more recently in contryphan-Vc1, has been shown to possess remarkable thermal, conformational, and chemical stability and can accept a short bioactive epitope without compromising the core structure of the peptide. In this study, we demonstrated that the single disulfide bond is critical in maintaining the native fold by replacing both cysteine residues with serine. We also designed an analogue with an additional, non-native disulfide bridge by replacing Gln1 and Tyr9 with Cys. Contryphan-Vc11–22[Q1C, Y9C] was synthesised utilising orthogonal cysteine protection and its solution structure determined using solution NMR spectroscopy. This analogue maintained the overall fold of native contryphan-Vc1. Previous studies had shown that the β-hairpin core of contryphan-Vc1 was resistant to proteolysis by trypsin and α-chymotrypsin but susceptible to cleavage by pepsin. Contryphan-Vc11–22[Q1C, Y9C] proved to be completely resistant to pepsin, thus confirming our design strategy. These results highlight the role of the disulfide bond in maintaining the SDH fold and provide a basis for the design of more stable analogues for peptide epitope grafting.

Solution Structure and Activity of the Synthetic Four-Disulfide Bond Mediterranean Mussel Defensin (MGD-1)

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14436-14447 ◽  
Author(s):  
Yin-Shan Yang ◽  
Guillaume Mitta ◽  
Alain Chavanieu ◽  
Bernard Calas ◽  
Jean Frédéric Sanchez ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Solution Structure ◽  
Mediterranean Mussel ◽  
Structure And Activity

scholarly journals Methoxyamine attack on cytosine produces ambivalent base pairing properties of the modified base.

1996 ◽  
Vol 43 (1) ◽  
pp. 95-105 ◽  
Author(s):  
Z Gdaniec ◽  
L C Sowers ◽  
G V Fazakerley
Keyword(s):  
Low Temperature ◽  
Methoxy Group ◽  
Solution Structure ◽  
Pair Formation ◽  
Single Strand ◽  
The Other ◽  
Base Pairing ◽  
Slow Exchange ◽  
Amino Form ◽  
Opposite Strand

We report the solution structure of two heptanucleotides each containing a central N4-methoxycytosine, in one case with adenine on the opposite strand and in the other with guanine. For the N4-methoxycytosine-adenine pair only the imino form of the N4-methoxycytosine residue is observed and base pairing is in Watson-Crick geometry. However, rotation of the methoxy group about the N-OCH3 bond is not constrained to a particular orientation although it must be anti to the N3 of N4-methoxycytosine. The slow exchange on a proton NMR time scale between the single strand and double strand forms is attributed to the strong preference of the syn conformation of the OCH3 group in the single strand which inhibits base pair formation. For N4-methoxycytosine base paired with guanosine we observe the N4-methoxycytosine base in the amino form in Watson-Crick geometry and a slow exchange of this species with an imino form base paired in wobble geometry. The amino form is predominant at low temperature whereas the imino form predominates above 40 degrees C. Our results point to preferential replacement of dTTP by N4-methoxycytosine in primer elongation.

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5
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