Protein design: From the aspect of water solubility and stability

R Qing, S Hao, E Smorodina, D Jin, A Zalevsky… - Chemical …, 2022 - ACS Publications
Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Advances in injectable self-healing biomedical hydrogels

Y Tu, N Chen, C Li, H Liu, R Zhu, S Chen, Q Xiao, J Liu… - Acta Biomaterialia, 2019 - Elsevier
In recent years, implantable biomaterials have attracted significant interest owing to their
potentials for use in the therapy of physical defects and traumas. Among the implantable …

Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu

M Poudyal, K Patel, L Gadhe, AS Sawner… - Nature …, 2023 - nature.com
Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon
underlying the sequestration of macromolecules (such as proteins and nucleic acids) into …

De novo design of a fluorescence-activating β-barrel

J Dou, AA Vorobieva, W Sheffler, LA Doyle, H Park… - Nature, 2018 - nature.com
The regular arrangements of β-strands around a central axis in β-barrels and of α-helices in
coiled coils contrast with the irregular tertiary structures of most globular proteins, and have …

The amyloid state and its association with protein misfolding diseases

TPJ Knowles, M Vendruscolo… - Nature reviews Molecular …, 2014 - nature.com
The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

De novo protein design, a retrospective

IV Korendovych, WF DeGrado - Quarterly reviews of biophysics, 2020 - cambridge.org
Proteins are molecular machines whose function depends on their ability to achieve
complex folds with precisely defined structural and dynamic properties. The rational design …

De novo design of transmembrane β barrels

AA Vorobieva, P White, B Liang, JE Horne, AK Bera… - Science, 2021 - science.org
INTRODUCTION Despite their key biological roles, only a few proteins that fold into lipid
membranes have been designed de novo. A class of membrane proteins—transmembrane …

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

M Biancalana, S Koide - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2010 - Elsevier
Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of
amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since …

Principles for designing ideal protein structures

N Koga, R Tatsumi-Koga, G Liu, R Xiao, TB Acton… - Nature, 2012 - nature.com
Unlike random heteropolymers, natural proteins fold into unique ordered structures.
Understanding how these are encoded in amino-acid sequences is complicated by …

Structure of the cross-β spine of amyloid-like fibrils

R Nelson, MR Sawaya, M Balbirnie, AØ Madsen… - Nature, 2005 - nature.com
Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common
properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and …