TY - JOUR
T1 - Folding of small disulfide-rich proteins: clarifying the puzzle
AU - Arolas, Joan L.
AU - Aviles, Francesc X.
AU - Chang, Jui Yoa
AU - Ventura, Salvador
PY - 2006/5/1
Y1 - 2006/5/1
N2 - The process by which small proteins fold to their native conformations has been intensively studied over the past few decades. The particular chemistry of disulfide-bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high level of diversity in folding mechanisms, differing in the heterogeneity and native disulfide-bond content of their intermediates. Information from folding studies of these proteins, together with the recent structural determinations of predominant intermediates, has provided new molecular insights into oxidative folding and clarifies the major rules that govern it. © 2006 Elsevier Ltd. All rights reserved.
AB - The process by which small proteins fold to their native conformations has been intensively studied over the past few decades. The particular chemistry of disulfide-bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high level of diversity in folding mechanisms, differing in the heterogeneity and native disulfide-bond content of their intermediates. Information from folding studies of these proteins, together with the recent structural determinations of predominant intermediates, has provided new molecular insights into oxidative folding and clarifies the major rules that govern it. © 2006 Elsevier Ltd. All rights reserved.
UR - https://ddd.uab.cat/record/67768
U2 - https://doi.org/10.1016/j.tibs.2006.03.005
DO - https://doi.org/10.1016/j.tibs.2006.03.005
M3 - Review article
VL - 31
SP - 292
EP - 301
IS - 5
ER -