Beyond amino acid sequence: disulfide bonds and the origins of the extreme amyloidogenic properties of insulin's H‐fragment
The presence of disulfide bonds affects the protein stability and therefore tendency to
misfold and form amyloid‐like fibrils. Insulin's three disulfide bridges stabilize the native state …
misfold and form amyloid‐like fibrils. Insulin's three disulfide bridges stabilize the native state …
Beyond amino acid sequence: disulfide bonds and the origins of the extreme amyloidogenic properties of insulin's H-fragment
R Dec, M Koliński, W Dzwolak - The FEBS journal, 2019 - pubmed.ncbi.nlm.nih.gov
The presence of disulfide bonds affects the protein stability and therefore tendency to
misfold and form amyloid-like fibrils. Insulin's three disulfide bridges stabilize the native state …
misfold and form amyloid-like fibrils. Insulin's three disulfide bridges stabilize the native state …
Beyond amino acid sequence: disulfide bonds and the origins of the extreme amyloidogenic properties of insulin's H-fragment.
R Dec, M Koliński, W Dzwolak - The FEBS Journal, 2019 - europepmc.org
The presence of disulfide bonds affects the protein stability and therefore tendency to
misfold and form amyloid-like fibrils. Insulin's three disulfide bridges stabilize the native state …
misfold and form amyloid-like fibrils. Insulin's three disulfide bridges stabilize the native state …