Article
Multidisciplinary Sciences
Kristen A. Gaffney, Ruiqiong Guo, Michael D. Bridges, Shaima Muhammednazaar, Daoyang Chen, Miyeon Kim, Zhongyu Yang, Anthony L. Schilmiller, Nabil F. Faruk, Xiangda Peng, A. Daniel Jones, Kelly H. Kim, Liangliang Sun, Wayne L. Hubbell, Tobin R. Sosnick, Heedeok Hong
Summary: Defining the denatured state ensemble (DSE) and disordered proteins is crucial for understanding various cellular processes. This study focuses on characterizing the DSE of the helical membrane protein GlpG in Escherichia coli using different techniques including limited proteolysis, mass spectrometry, and double electron-electron resonance spectroscopy. The obtained data suggest that the DSE is highly dynamic, involving topological changes and unfolding of some transmembrane helices. Additionally, the expansion of the DSE is influenced by protein packing and lipid composition.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Multidisciplinary Sciences
R. Charlotte Eccleston, David D. Pollock, Richard A. Goldstein
Summary: Epistasis and cooperativity in protein folding are both influenced by networks of energetic interactions within proteins, and their selection can affect each other. Selection for cooperativity may be crucial for predicting protein structure using epistasis measurements.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Review
Endocrinology & Metabolism
Balamurugan Dhayalan, Deepak Chatterjee, Yen-Shan Chen, Michael A. Weiss
Summary: Analysis of diabetes-associated mutations in the human insulin gene has provided insights into the folding mechanisms of proinsulin, revealing the impact of mutations on pancreatic beta-cell dysfunction and insulin secretion. Studies suggest that conserved residues play a crucial role in folding efficiency and the susceptibility of proinsulin to impaired foldability can contribute to the development of diseases. This highlights the molecular links between biophysical principles and the impact on diseases such as diabetes and obesity.
FRONTIERS IN ENDOCRINOLOGY
(2021)
Article
Chemistry, Multidisciplinary
Sandhya Bhatia, Guruswamy Krishnamoorthy, Jayant B. Udgaonkar
Summary: The study investigates the multiple folding pathways of a protein by characterizing the folding landscape of monellin using time-resolved FRET methodology. The research reveals that structure formation in protein folding can progress through parallel pathways, with different protein segments acquiring structure independently of each other. A phenomenological model is proposed to describe the sequence of structural acquisition in different subensembles of protein molecules.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Food Science & Technology
Theodore Sentoukas, Garoufalia Charitou, Janine Wagner, Anja Maria Wagemans, Thomas Moschakis, Aristeidis Papagiannopoulos
Summary: This study introduces a novel method for producing protein nanoparticles by denaturing whey protein isolate with ethanol. The results showed that the controlled concentration of ethanol allows for the production of different nanoparticles within specific pH ranges. Ethanol denaturation presents a promising technique for forming protein nanoparticles, with great potential for applications.
FOOD STRUCTURE-NETHERLANDS
(2023)
Article
Biology
Masahiro Noji, Tatsushi Samejima, Keiichi Yamaguchi, Masatomo So, Keisuke Yuzu, Eri Chatani, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yasushi Kawata, Kensuke Ikenaka, Hideki Mochizuki, Jozsef Kardos, Daniel E. Otzen, Vittorio Bellotti, Johannes Buchner, Yuji Goto
Summary: Noji et al. test the link between protein folding and misfolding upon heating and agitation, showing that folding and amyloid formation are separated by the supersaturation barrier of a protein, breakdown of which shifts the protein to the amyloid pathway. This study is valuable for understanding protein folding versus self-assembly and amyloidogenesis.
COMMUNICATIONS BIOLOGY
(2021)
Article
Chemistry, Multidisciplinary
Rishika Aggrawal, Sayantan Halder, Shalini Dyagala, Subit K. Saha
Summary: This study investigates the binding interactions between sodium dodecyl sulphate (SDS) and conjugated gold nanoparticles-bovine serum albumin (BSA) and explores their refolding process. The results show that the relaxed bioconjugates renature by removing bound gemini surfactants as the SDS concentration increases. The presence of 12-8-12,2Br(-) leads to more refolding induced by SDS. These findings are significant for understanding distance-dependent optical biomolecular detection methodologies and physicochemical properties.
Article
Chemistry, Multidisciplinary
Andrew Stannard, Marc Mora, Amy E. M. Beedle, Marta Castro-Lopez, Stephanie Board, Sergi Garcia-Manyes
Summary: Molecular fluctuations reveal the energy landscape of proteins, with variance analysis showing that unfolding and refolding transitions in proteins under mechanical forces result in changes in protein stiffness. The study demonstrates that the change in protein compliance with force-induced thermodynamically stable states is proportional to the protein's contour length increment, in line with the freely jointed chain model in polymer physics. These findings provide insights into the conformational dynamics of proteins under mechanical force which are crucial for mechanosensing and mechanotransduction.
Article
Biochemistry & Molecular Biology
Nan Xiao, Hongming Ma, Hong Gao, Jing Yang, Dan Tong, Dingzhu Gan, Jinhua Yang, Chi Li, Kang Liu, Yingxin Li, Zhibo Chen, Chaoqun Yin, Xingqi Li, Hongwu Wang
Summary: Liver cancer can be primary or secondary, with higher incidence of the latter. Despite advances in molecular biology and treatments, liver cancer still has a poor prognosis with no cure. Many questions remain regarding the mechanisms of liver cancer occurrence and development, as well as tumor reoccurrence after treatment.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Materials Science, Multidisciplinary
Ranajit Barman, Priya Rajdev, Tathagata Mondal, Pradip Dey, Suhrit Ghosh
Summary: This article presents the synthesis of thermoresponsive alternating copolymers based on a segmented polyurethane scaffold. The polymers exhibit a lower critical solution temperature (LCST) and can form hollow capsules capable of sequestering hydrophilic guests. The LCST can be tuned by adjusting the degree of polymerization (DP) or hydrophobic/hydrophilic balance. The polymeric system shows excellent biocompatibility and has potential applications as a delivery vehicle in biomedical fields.
ACS APPLIED POLYMER MATERIALS
(2022)
Review
Polymer Science
Zahoor Ahmad Parray, Mohammad Shahid, Asimul Islam
Summary: Proteins are essential for cellular communication and metabolism, and their structure plays a crucial role in the development of cells and tissues. The folding of proteins into a specific three-dimensional structure is determined by their characteristic sequence of amino acids. Intermediate states that occur during the folding process are significant for cellular functions. It is important to characterize these intermediate species in order to understand the folding pathways and machinery of proteins. In this review article, the various intermediate states observed and characterized in vitro conditions are discussed, along with their role in regulating the biological function of cells.
Article
Biochemistry & Molecular Biology
Jiaan Yang, Wen Xiang Cheng, Xiao Fei Zhao, Gang Wu, Shi Tong Sheng, Qiyue Hu, Hu Ge, Qianshan Qin, Xinshen Jin, Lianshan Zhang, Peng Zhang
Summary: Protein folding is a challenging subject, and the discovery of protein structural flexibility is another major hurdle. Researchers have developed a novel approach, protein structure fingerprint, to expose local folding variations and construct folding conformations for the entire protein. Through the creation of a database and the use of Protein Folding Variation Matrix (PFVM), all folding variations for an entire protein can be simultaneously understood, and the most likely folding conformation and 3D structure can be determined. This approach provides a significant means for investigating the protein folding problem.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
(2022)
Article
Biochemistry & Molecular Biology
Harsimranjit Sekhon, Jeung-Hoi Ha, Stewart N. Loh
Summary: Protein conformational switches can be constructed by fusing an input domain that recognizes a target ligand to an output domain that establishes a biological response. This study successfully converted the ribonuclease barnase to a switchable enzyme by duplicating a portion of its sequence and adding FK506 binding protein copies, resulting in complementary folding events that activate the enzyme's function.
FRONTIERS IN MOLECULAR BIOSCIENCES
(2023)
Article
Engineering, Mechanical
Xuming Niu, Xubo Yao, Yan Liu, Zhigang Sun, Yingdong Song
Summary: This study investigated the fatigue mechanical properties of SiCf/Ti composites under a spectrum load and performed a fatigue test on SiCf/Ti composites under spectrum load, followed by analyzing the failure mechanism. The evolution of typical damage modes, including fiber breakage, matrix cracking, and interface wear, with the number of spectrum load cycles was studied by establishing a fatigue damage model for each type of damage under spectrum load. The fatigue hysteresis loop, residual stiffness, and residual strength were simulated and compared with practical experiments using the combination of the meso-mechanical model and fatigue damage model.
INTERNATIONAL JOURNAL OF FATIGUE
(2023)
Article
Biochemistry & Molecular Biology
Ryosuke Tomiyama, Masatomo So, Keiichi Yamaguchi, Yohei Miyanoiri, Kazumasa Sakurai
Summary: β(2)-Microglobulin can form amyloid fibrils in acidic conditions. The presence of disulfide bonds affects the residual structure of the monomer, which influences the morphology of the fibrils.
Article
Biochemistry & Molecular Biology
Ankita Chadda, Alexander G. Kozlov, Binh Nguyen, Timothy M. Lohman, Eric A. Galburt
Summary: In this study, it was found that the DNA damage response in Mycobacterium tuberculosis differs from well-studied model bacteria. The DNA repair helicase UvrD1 in Mtb is activated through a redox-dependent process and is closely associated with the homo-dimeric Ku protein. Additionally, Ku protein is shown to stimulate the helicase activity of UvrD1.
JOURNAL OF MOLECULAR BIOLOGY
(2024)