Tag: Molecular biology

Learn how to search GenBank effectively using accession numbers, organism names, gene names, sequence types, filters, and other search strategies to find relevant nucleotide sequences.

Protein aggregation occurs when protein molecules associate to form larger structures. Learn about aggregation mechanisms, nucleation, amyloid structures, molecular chaperones, proteostasis, disease research, and biotechnology.

Protein misfolding occurs when proteins fail to achieve or maintain their correct three-dimensional structures. Learn about its causes, protein aggregation, cellular quality control, biological consequences, and scientific importance.

Protein folding is the process through which amino acid chains form functional three-dimensional structures. Learn about folding mechanisms, molecular forces, chaperones, protein misfolding, stability, disease, and biotechnology.

Discover the four levels of protein structure: primary, secondary, tertiary, and quaternary. Learn how amino acid sequences form complex three-dimensional proteins and influence biological function.

Discover the history and development of the Protein Data Bank (PDB), from its establishment in 1971 to its evolution into a global scientific archive supporting structural biology, medicine, bioinformatics, and drug discovery.

The Protein Data Bank (PDB) is a global open-access resource containing three-dimensional structures of proteins, DNA, RNA, and other biological macromolecules. Discover its history, structure determination methods, applications, and importance in modern science.

Protein sulfation is an important modification that regulates protein interactions, cell adhesion, extracellular signaling, immune responses, coagulation, and tissue organization. Explore tyrosine sulfation, glycosaminoglycan sulfation, sulfotransferases, PAPS, and their roles in health and disease.

Post-translational modifications are essential regulators of cell-cycle progression. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control CDKs, cyclins, checkpoints, DNA replication, mitosis, and protein degradation.

Protein neddylation is an important post-translational modification involving the attachment of NEDD8 to target proteins. Learn how neddylation regulates cullin-RING ubiquitin ligases, protein degradation, cell-cycle progression, DNA repair, cellular signaling, and cancer biology.

Protein hydroxylation is an important post-translational modification that regulates protein structure, stability, folding, molecular interactions, and cellular signaling. Explore proline, lysine, and asparagine hydroxylation, collagen maturation, oxygen sensing, HIF signaling, and disease.

Post-translational modifications are essential regulators of cell migration. Discover how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and lipid modifications control cytoskeletal dynamics, focal adhesions, cell polarity, and cancer invasion.

Post-translational modifications are essential regulators of apoptosis. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control p53, BCL-2 proteins, caspases, mitochondrial apoptosis, and cell survival.

Protein nitrosylation is an important redox-dependent post-translational modification, with S-nitrosylation regulating cysteine residues and influencing protein activity, signaling, metabolism, mitochondrial function, immunity, and disease.

Protein carbonylation is an important oxidative post-translational modification associated with reactive oxygen species, oxidative stress, protein damage, aging, mitochondrial dysfunction, inflammation, and disease. Learn how carbonylated proteins form, affect cellular function, and are detected.