Article
Multidisciplinary Sciences
Jingyao Li, Bojing Jiang, Xinyuan Chang, Han Yu, Yichao Han, Fuzhong Zhang
Summary: The authors have developed a method to enhance the strength of low molecular-weight protein materials by fusing intrinsically-disordered mussel foot protein fragments. This approach can be applied to a wide range of protein-based materials and has the potential to achieve high yields.
NATURE COMMUNICATIONS
(2023)
Review
Biochemistry & Molecular Biology
Rakesh Trivedi, Hampapathalu Adimurthy Nagarajaram
Summary: This review discusses different aspects of disordered proteins and protein regions, as well as the experimental and computational methods used to characterize them. Additionally, the role of disordered proteins in diseases and their potential as drug targets are explored.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Chemistry, Multidisciplinary
Guy Jacoby, Merav Segal Asher, Tamara Ehm, Inbal Abutbul Ionita, Hila Shinar, Salome Azoulay-Ginsburg, Ido Zemach, Gil Koren, Dganit Danino, Michael M. Kozlov, Roey J. Amir, Roy Beck
Summary: This study introduces a new type of peptide amphiphiles, intrinsically disordered peptide amphiphiles (IDPA), that exhibit a sharp pH-induced micellar phase-transition. The shape transition can serve as a mechanism for the design of cargo hold-and-release applications, demonstrating the potential of tailoring interactions between disordered peptides for various stimuli-responsive biomedical applications.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Nanoscience & Nanotechnology
Noriyuki Kodera, Daisuke Noshiro, Sujit K. Dora, Tetsuya Mori, Johnny Habchi, David Blocquel, Antoine Gruet, Marion Dosnon, Edoardo Salladini, Christophe Bignon, Yuko Fujioka, Takashi Oda, Nobuo N. Noda, Mamoru Sato, Marina Lotti, Mineyuki Mizuguchi, Sonia Longhi, Toshio Ando
Summary: High-speed atomic force microscopy imaging can provide a semiquantitative, realistic description of the dynamic structure of intrinsically disordered proteins, which dynamically sample a multitude of conformational states, making their structural analysis difficult.
NATURE NANOTECHNOLOGY
(2021)
Review
Biochemistry & Molecular Biology
Kiersten M. Ruff, Rohit Pappu
Summary: Accurate predictions of protein structures using AlphaFold have made significant progress. Most protein sequences in the human proteome have been structurally annotated, with over 30% of regions being disordered.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Review
Cell Biology
Alex S. Holehouse, Birthe B. Kragelund
Summary: Intrinsically disordered protein regions, lacking a stable 3D structure, are structurally heterogeneous and widely present in all kingdoms of life. Despite their lack of a defined structure, these regions play essential roles in cellular processes and can be regulated by their structural and chemical context. Recent studies have advanced our understanding of the link between protein sequence and conformational behavior in disordered regions, but the connection between sequence and molecular function is still not well defined.
NATURE REVIEWS MOLECULAR CELL BIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
H. Jane Dyson
Summary: Viruses infect all kingdoms of life and employ disordered proteins to accomplish various functions. Disordered proteins have been discovered in almost all viruses studied, regardless of the viral genome composition or the viral capsid configuration. This review presents a collection of stories illustrating the diverse functions of disordered proteins in viruses, providing a survey of the field's expansion.
JOURNAL OF MOLECULAR BIOLOGY
(2023)
Article
Chemistry, Physical
Samuel Wohl, Matthew Jakubowski, Wenwei Zheng
Summary: The study introduced a new model to explain the influence of salt on protein structure, revealing the significant role of salting-out effect in IDP sequences, especially those with moderately charged residues. This model also shows general applicability in conformation studies of other proteins.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2021)
Review
Biochemistry & Molecular Biology
Rachel Evans, Sravani Ramisetty, Prakash Kulkarni, Keith Weninger
Summary: Intense study of intrinsically disordered proteins (IDPs) began in the late 1990s and revealed their important functions. Over the past two decades, it has become clear that IDPs play critical roles in various biological phenomena. The application of integrative structural biology has emerged as an essential approach to understanding IDP phenomena.
Article
Biochemistry & Molecular Biology
Estella A. Newcombe, Catarina B. Fernandes, Jeppe E. Lundsgaard, Inna Brakti, Kresten Lindorff-Larsen, Annette E. Langkilde, Karen Skriver, Birthe B. Kragelund
Summary: Motifs within proteins help categorize their functions;Intrinsically disordered proteins (IDPs) rich in short linear motifs with various roles;Study found calcium-binding motifs in IDPs may serve various underreported structural and functional roles.
Article
Biochemistry & Molecular Biology
Tamara Ehm, Hila Shinar, Guy Jacoby, Sagi Meir, Gil Koren, Merav Segal Asher, Joanna Korpanty, Matthew P. Thompson, Nathan C. Gianneschi, Michael M. Kozlov, Salome Azoulay-Ginsburg, Roey J. Amir, Joachim O. Raedler, Roy Beck
Summary: Intrinsically disordered peptide amphiphiles (IDPAs) are a novel class of synthetic conjugates that self-assemble into dispersed nanoscopic aggregates or ordered mesophases. Sequence variations in the IDPA systems can significantly alter the headgroup conformation and induce phase transitions, and alterations in the peptide sequence can render IDPAs susceptible to enzymatic cleavage and induce enzymatically activated phase transitions.
Review
Chemistry, Multidisciplinary
Prakash Kulkarni, Supriyo Bhattacharya, Srisairam Achuthan, Amita Behal, Mohit Kumar Jolly, Sourabh Kotnala, Atish Mohanty, Govindan Rangarajan, Ravi Salgia, Vladimir Uversky
Summary: This article discusses the knowledge and unknown areas of intrinsically disordered proteins (IDPs), and explores the influence of IDPs on cell-fate decisions, as well as their potential roles in cellular phenotype switching, biological evolution, proteinaceous organelle formation, and transgenerational inheritance.
Review
Biochemistry & Molecular Biology
Goro Kato
Summary: This review discusses the structural and functional aspects of Src protein and its regulatory mechanism. By reviewing nuclear magnetic resonance analyses and recent studies, the authors explore new characteristics and regulatory roles of Src protein. Finally, the new regulatory roles are integrated with the canonical model to elucidate the functions of full-length Src.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Multidisciplinary Sciences
Feng Yuan, Christopher T. Lee, Arjun Sangani, Justin R. Houser, Liping Wang, Eileen M. Lafer, Padmini Rangamani, Jeanne C. Stachowiak
Summary: Membrane curvature is crucial for cellular functions and recent studies have revealed the role of intrinsically disordered proteins in driving membrane bending. Repulsive interactions among disordered domains lead to convex curvature, while attractive interactions result in concave curvature, forming membrane-bound liquid-like condensates. This study investigates the effects of disordered domains containing both repulsive and attractive interactions on curvature. The findings show that the position of the attractive or repulsive domain relative to the membrane determines the curvature, with increasing ionic strength altering the transition from convex to concave. These results provide design rules for membrane bending by disordered proteins.
Article
Materials Science, Multidisciplinary
Maryam Rahmati, Sabine Stoetzel, Thaqif El Khassawna, Chenyi Mao, Adilijiang Ali, Joshua C. Vaughan, Kamila Iskhahova, D. C. Florian Wieland, Antonio Gonzalez Cantalapiedra, Giuseppe Perale, Felice Betge, Eoghan P. Dillon, Stale Petter Lyngstadaas, Havard Jostein Haugen
Summary: Biomaterial scientists have designed organic bone substitutes based on the biochemical properties of the tissue they mimic, aiming to achieve similar functionality. In this study, two proline-rich disordered peptides (P2 and P6) were incorporated into a biohybrid substitute called SmartBone (R) (SBN). The results showed that these peptides can stimulate bone formation and biomineralization, with P6 being more effective in the early stages while P2 had a stronger effect on later processes. Furthermore, the use of various analysis techniques proved to be valuable in evaluating and diagnosing the structure of bone tissue and the bone-biomaterial interface.