TY - JOUR
T1 - Disulfide bond formation in peptides.
AU - Chen, L.
AU - Annis, I.
AU - Barany, G.
N1 - Copyright:
This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine
PY - 2001/5
Y1 - 2001/5
N2 - The formation of disulfide bridges is often a crucial final stage in peptide synthesis. There is compelling evidence that the disulfide pattern can be critical in the folding and structural stabilization of many natural peptide and protein sequences, while the artificial introduction of disulfide bridges into natural or designed peptides may often improve biological activities/specificities and stabilities. This unit provides a highly selective, albeit state-of-the-art, menu of procedures that can be performed to establish intramolecular or intermolecular disulfide bridges in targets of varying complexities.
AB - The formation of disulfide bridges is often a crucial final stage in peptide synthesis. There is compelling evidence that the disulfide pattern can be critical in the folding and structural stabilization of many natural peptide and protein sequences, while the artificial introduction of disulfide bridges into natural or designed peptides may often improve biological activities/specificities and stabilities. This unit provides a highly selective, albeit state-of-the-art, menu of procedures that can be performed to establish intramolecular or intermolecular disulfide bridges in targets of varying complexities.
UR - http://www.scopus.com/inward/record.url?scp=44949085744&partnerID=8YFLogxK
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U2 - 10.1002/0471140864.ps1806s23
DO - 10.1002/0471140864.ps1806s23
M3 - Article
C2 - 18429142
AN - SCOPUS:44949085744
SN - 1934-3655
VL - Chapter 18
SP - Unit18.6
JO - Current protocols in protein science / editorial board, John E. Coligan ... [et al.]
JF - Current protocols in protein science / editorial board, John E. Coligan ... [et al.]
ER -