The introduction of disulfide bonds and a change in conformation between the cis and trans conformations of the proline peptide bond may be a barrier to the rapid formation of the proper protein structure. In the cell, enzymes are present to catalyse these processes.Key Concepts:The ...
Archives of Biochemistry and Biophysics Volume 76, Issue 1, July 1958, Pages 161-167Absorption spectrum of the peptide bond: Basic properties of peptides and proteins☆ Author links open overlay panelA.R. Goldfarb, E. Hoffmann 2, N. GutsteinShow more Add to Mendeley Share Cite...
Properties of Peptide Bond An amino acid fused in a peptide chain loses one H (of its NH2) and one Goodness (of its COOH), or just one of the two in the event that it is a terminal amino acid. This is called an amino acid "buildup"; it is assigned by adding the addition "yl...
The second derivative of the ultraviolet spectrum has two peaks and troughs compared with the relatively uncharacteristic ultraviolet spectrum, mainly caused by the electronic transition of peptide bonds. It reflects the conformation of the main chain of the peptide chain, can better reflect the change...
Disulfide bond formation in peptides The goal of this review has been to present different chemical approaches for the formation of disulfide bonds in synthetic peptides and small proteins. Th... I Annis,B Hargittai,G Barany - 《Methods in Enzymology》 被引量: 238发表: 1997年 ...
of control over interfacial biointeractions. Protein-surface interactions are thought to be of particular importance due to the abundance of these molecules in tissues and biological fluids and due to the central role of peptides and proteins in cell adhesion and signalling. Depending on the ...
Large-scale application of free energy perturbation calculations for antibody design Article Open access 21 July 2022 Electrostatic complementarity at the interface drives transient protein-protein interactions Article Open access 23 June 2023 Peptide binder design with inverse folding and protein struct...
However, both Cono-1 and Cono-2 are considerably less structured than α-conotoxin GI, which indicates that formation of the second disulfide bond to give the Cys2−Cys7, Cys3−Cys13 pairing induces considerable structure into the backbone of the peptide. 展开 ...
The addition of another electron to O2•− produces O2−, the peroxide ion, a non-radical (no unpaired electrons) with a weaker oxygen–oxygen bond. The addition of another two electrons to O22− completely eliminates the bond, producing two O2− (oxide ions). In biology, the two...
The N-terminal sequence of human serum albumin (HSA) is known as a metal binding site, such as for Co2+, Cu2+, and Ni2+. For this study, we designed and synthesized wAlb12 peptide from the N-terminal region of HSA, which can bind to cobalt, to develop a peptide-based chelate. ...