Together, these results show that designed repeat-protein folding is governed by seed formation, interface propagation, and terminal boundary conditions, and establish intramolecular crosslinking as a strategy for rationally reshaping folding landscapes in designed proteins.
The structural feasibility of chain folding within an accepted cellulose-II structure is investigated in this study. We incorporate 3-residue and 5-residue folded glucosyl turns into a cellulose-II fibril crystal model to assess if the dominant structure can be retained. Ten candidate turn models were generated by meta...
Ling-Han Kong, S. J. Eichhorn, Richard A. Bryce· Biomacromolecules· 0 citations
Protein folding is the process by which a polypeptide chain organizes into its three-dimensional structure through a balance of stabilizing and destabilizing interactions encoded by the sequence. A central question in protein biophysics is how thermodynamic factors guide a polypeptide toward its native folded state des...
The answer lies in geometry: proteins with denser cores, larger size, and higher-order oligomeric assembly tolerate mutations more readily, occupy larger structural families, and support more versatile biological roles, reveals that protein size, shape, and self-assembly, not just sequence, are fundamental drivers of e...
De novo protein design is advancing rapidly1,2. This is being driven by AI to generate protein backbones, sequences, and structural models3–7. As a result, de novo designed proteins are becoming larger and more complex8–10, and increasingly explore new protein structures11,12. By contrast, natural proteins have evolved...
K. I. Albanese, Joel J. Chubb, L. Gutierrez-Rus et al.· bioRxiv· 0 citations
A mechanistic model of de novo folding initiation during biosynthesis is infer and a complete atomistic description of a co-translational folding pathway is provided by linking the folding nucleus to downstream partially structured intermediates and the native state is provided.
Ivana V. Bukvin, Julian O. Streit, Tomasz Włodarski et al.· bioRxiv· 0 citations
Together, these insights position conformational dynamics at the center of understanding and engineering the evolutionary logic of protein function, opening the door to study how proteins are tuned to operate under the nonequilibrium conditions of living cells.
Sixto M. Herrera, Elías Manríquez-Benítez, Exequiel Medina· Current Opinion in Structura...· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
