FOXP3FOXP3 (forkhead box P3), also known as scurfin, is a protein involved in immune system responses. A member of the FOX protein family, FOXP3 appears to function as a master regulator of the regulatory pathway in the development and function of regulatory T cells. Regulatory T cells generally turn the immune response down. In cancer, an excess of regulatory T cell activity can prevent the immune system from destroying cancer cells. In autoimmune disease, a deficiency of regulatory T cell activity can allow other autoimmune cells to attack the body's own tissues.
AnnexineInfobox Famille de protéines | nom = Annexine | image = 1aei.jpg | légende = Hexamère d'annexine dHydra vulgaris'' () | Pfam = PF00191 | Clan_Pfam = | InterPro = IPR001464 | SMART = | PROSITE = PDOC00195 | MEROPS = | SCOP = 2ran | TCDB = 1.A.31 | Famille_OPM = 41 | Proteine_OPM = 1w3w | CAZy = | CDD = Les annexines (ou lipocortines''') sont une famille de protéines intervenant dans l'inflammation et l'apoptose. Elles sont présentes dans de nombreuses cellules eucaryotes.
Doigt de zincthumb|Dessin représentant le doigt de zinc Cys2His2, consistant en une hélice alpha et un feuillet bêta aux brins antiparallèles. L'ion zinc est en vert, complexé à deux histidines (en bas) et deux cystéines (en haut, soufre en doré) Les doigts de zinc sont de petits motifs structuraux trouvés dans les protéines et capables d'ordonner en complexe un ou plusieurs ions zinc pour stabiliser leur repliement.
SH2 domainThe SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein. The SH2 domain may be considered the prototypical modular protein-protein interaction domain, allowing the transmission of signals controlling a variety of cellular functions.
Protein crystallizationProtein crystallization is the process of formation of a regular array of individual protein molecules stabilized by crystal contacts. If the crystal is sufficiently ordered, it will diffract. Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye. In the process of protein crystallization, proteins are dissolved in an aqueous environment and sample solution until they reach the supersaturated state. Different methods are used to reach that state such as vapor diffusion, microbatch, microdialysis, and free-interface diffusion.
Protein fold classIn molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). Four large classes of protein that are generally agreed upon by the two main structure classification databases (SCOP and CATH).
Macromolecular assemblyThe term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially (i.e., with regard to their chemical shape), and with regard to their underlying chemical composition and structure.
Protéine antigelLes protéines antigel sont des qui correspondent à une classe de polypeptides naturellement produites par certaines espèces de vertébrés à sang froid, de plantes, de fungis et de bactéries et qui leur permettent d'être congelés sans mourir et/ou de vivre activement dans des environnements très froids (jusqu'à des températures inférieures à , dans l'eau de mer par exemple). Elles sont souvent nommées AFPs (de l'anglais : Antifreeze proteins).
Faisceau d'hélicesvignette|Exemple de faisceau de trois hélices, formant le domaine en casque d'une villine de poulet (). Un faisceau d'hélices (helix bundle en anglais) est une petite structure tertiaire de certaines protéines constituée de plusieurs hélices α généralement parallèles ou antiparallèles entre elles. Les faisceaux de trois hélices comptent parmi les domaines structuraux à la fois les plus petits et les plus rapides à se replier de manière coopérative.
Equilibrium unfoldingIn biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, pH, adding chemical denaturants, or applying force as with an atomic force microscope tip. If the equilibrium was maintained at all steps, the process theoretically should be reversible during equilibrium folding. Equilibrium unfolding can be used to determine the thermodynamic stability of the protein or RNA structure, i.e.
