The membrane-binding characteristics of six vitamin K dependent plasma proteins, which have homologous amino acid sequences, were compared. All of these proteins display calcium-dependent membrane binding and the identified equilibria for protein-membrane binding are qualitatively the same for all proteins. Quantitative characteristics of these protein-membrane interactions allow organization into distinct subgroups. Protein C and factor VII form a subgroup which has extemely low affinity for bilayer membranes; prothrombin, factor X, and protein S form the tightest complexes with membranes and factor IX displays intermediate affinity. In the presence of manganese (which substitutes for calcium in a cation-dependent protein transition), calcium titration of protein-membrane binding shows the same calcium dependence for all proteins except prothrombin which requires lower calcium. These protein-membrane binding characteristics agree very well with the relatedness of these proteins based on their partial amino-terminal sequences.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/bi00604a017 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Mechanistic Insights into Synaptotagmin-1 Mediated Membrane Fusion and Interactions.
Methods Mol Biol
January 2025
Institute of Physical Chemistry, University of Göttingen, Göttingen, Germany.
We present two innovative approaches to investigate the dynamics of membrane fusion and the strength of protein-membrane interactions. The first approach employs pore-spanning membranes (PSMs), which allow for the observation of protein-assisted fusion processes. The second approach utilizes colloidal probe microscopy with membrane-coated probes with reconstituted proteins.
View Article and Find Full Text PDFFluorescence Anisotropy for Monitoring cis- and trans-Membrane Interactions of Synaptotagmin-1.
Methods Mol Biol
January 2025
Neurological Disorders Research Center, Qatar Biomedical Research Institute (QBRI), Hamad Bin Khalifa University (HBKU), Qatar Foundation, Doha, Qatar.
Vesicle fusion induces neurotransmitter release, orchestrated by synaptotagmin-1 (Syt-1) as a Ca sensor. However, the precise molecular mechanisms of Syt-1 remain controversial, with various and competing models proposed based on different ionic strengths. Syt-1, residing on the vesicle membrane alongside anionic phospholipids such as phosphatidylserine (PS), undergoes Ca-induced binding to its own vesicle membrane, known as the cis-interaction, which prevents the trans-interaction of Syt-1 with the plasma membrane.
View Article and Find Full Text PDFBioinformatics and Expression Profiling of the DHHC-CRD S-Acyltransferases Reveal Their Roles in Growth and Stress Response in Woodland Strawberry ().
Plants (Basel)
January 2025
School of Pharmacy and BioMolecular Sciences, Liverpool John Moores University, Byram Street, Liverpool L3 3AF, UK.
Protein S-acyl transferases (PATs) are a family of enzymes that catalyze protein S-acylation, a post-translational lipid modification involved in protein membrane targeting, trafficking, stability, and protein-protein interaction. S-acylation plays important roles in plant growth, development, and stress responses. Here, we report the genome-wide analysis of the family genes in the woodland strawberry (), a model plant for studying the economically important Rosaceae family.
View Article and Find Full Text PDFAtomistic Simulations and Analysis of Peripheral Membrane Proteins with Model Lipid Bilayers.
Methods Mol Biol
December 2024
Chemical and Biological Engineering Department, School of Engineering and Applied Sciences, State University of New York at Buffalo, Buffalo, NY, USA.
All-atom molecular dynamics (AAMD) is a computational technique that predicts the movement of particles based on the intermolecular forces acting on the system. It enables the study of biological systems at atomic detail, complements observations from experiments, and can help the selection of experimental targets. Here, we describe the applications of MD simulations to study the interaction between peripheral membrane proteins and lipid bilayers.
View Article and Find Full Text PDFUsing deep learning and large protein language models to predict protein-membrane interfaces of peripheral membrane proteins.
Bioinform Adv
May 2024
Biomedical Research Foundation, Academy of Athens, Athens 11527, Greece.
Motivation: Characterizing interactions at the protein-membrane interface is crucial as abnormal peripheral protein-membrane attachment is involved in the onset of many diseases. However, a limiting factor in studying and understanding protein-membrane interactions is that the membrane-binding domains of peripheral membrane proteins (PMPs) are typically unknown. By applying artificial intelligence techniques in the context of natural language processing (NLP), the accuracy and prediction time for protein-membrane interface analysis can be significantly improved compared to existing methods.
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!