The reductive cleavage of disulfide bonds and its application to problems of protein structure
References (33)
- et al.
J. Biol. Chem.
(1956) - et al.
J. Biol. Chem.
(1956) - et al.
J. Biol. Chem.
(1934) - et al.
- et al.
Advances in Protein Chem.
(1952) - et al.
Arch. Biochem. Biophys.
(1957) - et al.
Arch. Biochem. Biophys.
(1956) - et al.
J. Org. Chem.
(1952) - et al.
Biochem. J.
(1955)
Biochem. J.
Advances in Enzymol.
Chem. Rev.
J. Am. Chem. Soc.
J. Am. Chem. Soc.
Cited by (57)
All printed organic humidity sensor based on egg albumin
2020, Sensing and Bio-Sensing ResearchCitation Excerpt :The amino acids are classified into hydrophilic, hydrophobic, acidic, and basic, based on the tendency of side chain's linkage with water. A peptide bond is formed between two or multi amino acids when NH2 of one amino acid links with the COOH of other amino acid [23,32,33]. This reaction is known as dehydration reaction, as water is released during this reaction shown in Fig. 7(a).
Disulfidicity: A scale to characterize the disulfide bond strength via the hydrogenation thermodynamics
2012, Chemical Physics LettersCitation Excerpt :Ever since Anfinsen’s famous experiments [1,2], it is well known that the strength of the S–S linkage is an important parameter in protein folding and unfolding since cysteine (Cys) may not only be in its oxidized (QS–SQ), but also in its reduced (Q–SH) form as well.
Dynamic dissociating homo-oligomers and the control of protein function
2012, Archives of Biochemistry and BiophysicsCitation Excerpt :As crystal structures began to appear, other studies were emerging that supported the rigid protein view. Based on work started in the 1950s [49], Anfinsen and coworkers had established by the early 1970s that protein sequence alone can provide all the information necessary to specify the native three-dimensional structure of at least some proteins [50,51]. Implicit in Anfinsen’s principle is the assumption that there is only one physiologically relevant native structure, and presumably one native quaternary assembly.
Contributions of disulfide bonds in a nested pattern to the structure, stability, and biological functions of endostatin
2005, Journal of Biological ChemistryMy world through science
2004, Comprehensive BiochemistryFrom proteins and protein models to their use in immunology and immunotherapy
2003, Journal of Biological ChemistryCitation Excerpt :Oxidative opening of the four disulfide bridges of bovine pancreatic ribonuclease to permit its sequencing was possible only because tryptophan was absent in this protein. A more general method, which could be used also for a protein containing tryptophan, such as lysozyme, was reductive cleavage, followed by blocking of the sulfhydryl groups with iodoacetic acid (9). I was fortunate to participate with Chris in these studies and left part of the reduced ribonuclease without blocking its sulfhydryl groups to see if it could reoxidize properly and whether the enzymatic activity would come back.
- ★
On leave of absence from the Weizmann Institute of Science, Rehovot, Israel.