We found that that disulfide-bonding patterns can be used to discriminate structure similarity. Our method, based on the hierarchical clustering scheme, is applicable to proteins with two or more disulfide bonds and is able to detect the structural similarities of proteins of low sequence identities (<25%). Our results show the surprisingly close relationship between disulfide-bonding patterns and proteins structures. Our findings should be useful in protein structure modeling.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/prot.10492 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Changes in the structural, aggregation behavior and gel properties of pork myofibrillar protein induced by theaflavins.
Food Res Int
November 2024
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China. Electronic address:
This study explores the effect of different theaflavins (TFs) concentrations (0, 100, 300, 600 and 900 mg/L) on the structure, aggregation behavior and gelation properties of pork myofibrillar protein (MP). The protein structure and aggregation behavior were characterized by free sulfhydryl groups, surface hydrophobicity, fluorescence emission spectra, particle size and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The gel properties of samples were characterized by gel strength, cooking loss, microstructure and gel supernatant SDS-PAGE.
View Article and Find Full Text PDFCo-stabilization effects of gluten/carrageenan to the over-heated myofibrillar protein: Inhibit the undesirable gel weakening and protein over-aggregations.
Int J Biol Macromol
December 2024
College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China. Electronic address:
Article Synopsis
- - High-temperature sterilization (120 °C) for ready-to-eat surimi products can damage myofibrillar proteins, leading to weaker gelling properties.
- - A new strategy combining carrageenan (CG) with wheat gluten significantly improved the mechanical strength of protein gels, boosting their performance to four times stronger than untreated gels.
- - Different types of carrageenan resulted in varying gel strengths and moisture stabilization, offering insights into enhancing the quality of ready-to-eat meat products.
Effects of pasteurization temperature and amino acids on the gelation behavior of liquid egg yolk: Emphasizing rheology, gel properties, intermolecular forces and microstructure.
Food Chem
January 2025
College of Engineering, Northeast Agricultural University, Harbin 150030, China. Electronic address:
Pipeline blockage caused by liquid egg yolk (LEY) in the pasteurization process has become an urgent problem for egg industry. This study investigated the effects of amino acids (betaine/proline) on rheology of LEY and gel property of egg yolk gel (EYG) at various pasteurization temperatures (68, 72, and 76 °C). Rheological results revealed that 72 °C was the key transition point for increase in LEY thermal aggregation rate.
View Article and Find Full Text PDFBuffer Screening of Protein Formulations Using a Coarse-Grained Protocol Based on Medicinal Chemistry Interactions.
J Phys Chem B
October 2024
Siemens Industry Software Netherlands B.V., The Hague 2595 BN, The Netherlands.
In drug and vaccine development, the designed protein formulation should be highly stable against the temperature, pH, buffer, excipients, and other environmental settings. Similarly, in a sensing unit, one needs to know how strongly two biomolecules bind to guide the design of the biorecognition unit accordingly. Typically, the community performs a series of experiments to thoroughly examine the parameter space, the so-called design-of-experiment (DoE) method, to identify the optimal formulation conditions.
View Article and Find Full Text PDFA spectrum of clinically-identified cysteine mutations in fibulin-3 (EFEMP1) highlight its disulfide bonding complexity and potential to induce stress response activation.
bioRxiv
July 2024
Department of Ophthalmology and Visual Neurosciences, University of Minnesota, 2001 6 St. SE, Minneapolis, Minnesota, 55455, United States.
Fibulin-3 (FBLN3), also known as EFEMP1, is a secreted extracellular matrix (ECM) glycoprotein that contains forty cysteine residues. These cysteines, which are distributed across one atypical and five canonical calcium-binding epidermal growth factor (EGF) domains, are important for regulating FBLN3 structure, secretion, and presumably function. As evidence of this importance, a rare homozygous p.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!