Target type: biologicalprocess
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that results in the attainment of the full functional capacity of a protein. [GOC:isa_complete]
Protein maturation through protein folding is a fundamental biological process essential for the functionality and stability of proteins. It involves a complex interplay of forces that guide the polypeptide chain, synthesized as a linear sequence of amino acids, into a specific three-dimensional structure. This intricate process is driven by the hydrophobic effect, electrostatic interactions, hydrogen bonding, and van der Waals forces. Initially, the newly synthesized polypeptide chain emerges from the ribosome in an unfolded state, often referred to as a random coil. This unfolded state is unstable and prone to aggregation. As the chain emerges, chaperone proteins assist in preventing aggregation and guide the polypeptide towards its native conformation. The process of protein folding begins with the formation of local secondary structures, such as alpha-helices and beta-sheets, driven by interactions between amino acid side chains. These secondary structures then fold upon each other to form tertiary structures, stabilized by a variety of interactions including hydrogen bonding, hydrophobic interactions, electrostatic interactions, and disulfide bonds. For multi-subunit proteins, the tertiary structures assemble further to form quaternary structures, where multiple polypeptide chains interact to form a functional protein complex. Throughout the folding process, the protein can adopt intermediate states that may be either stable or unstable. Some proteins may require assistance from chaperone proteins to overcome energy barriers and reach their final conformation. Incorrect folding can lead to the formation of misfolded proteins, which can be detrimental to cellular function and can contribute to the development of diseases like Alzheimer's and Parkinson's. The process of protein folding is highly dynamic and influenced by various factors including temperature, pH, and the presence of other molecules. In summary, protein maturation through protein folding is a crucial process that ensures proteins achieve their correct shape and function, critical for the proper functioning of all living organisms.'
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Protein | Definition | Taxonomy |
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Peptidyl-prolyl cis-trans isomerase FKBP1B | A peptidyl-prolyl cis-trans isomerase FKBP1B that is encoded in the genome of human. [PRO:DNx, UniProtKB:P68106] | Homo sapiens (human) |
Peptidyl-prolyl cis-trans isomerase FKBP1A | A peptidyl-prolyl cis-trans isomerase FKBP1A that is encoded in the genome of human. [PRO:DNx, UniProtKB:P62942] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
thiabendazole | Tresaderm: dermatologic soln containing dexamethasone, thiabendazole & neomycin sulfate | 1,3-thiazoles; benzimidazole fungicide; benzimidazoles | antifungal agrochemical; antinematodal drug |
cycloheximide | cycloheximide : A dicarboximide that is 4-(2-hydroxyethyl)piperidine-2,6-dione in which one of the hydrogens attached to the carbon bearing the hydroxy group is replaced by a 3,5-dimethyl-2-oxocyclohexyl group. It is an antibiotic produced by the bacterium Streptomyces griseus. Cycloheximide: Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis. | antibiotic fungicide; cyclic ketone; dicarboximide; piperidine antibiotic; piperidones; secondary alcohol | anticoronaviral agent; bacterial metabolite; ferroptosis inhibitor; neuroprotective agent; protein synthesis inhibitor |
3-(3-pyridyl)-1-propyl-(2s)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-pyrrolidinecarboxylate | |||
tacrolimus | tacrolimus (anhydrous) : A macrolide lactam containing a 23-membered lactone ring, originally isolated from the fermentation broth of a Japanese soil sample that contained the bacteria Streptomyces tsukubaensis. Tacrolimus: A macrolide isolated from the culture broth of a strain of Streptomyces tsukubaensis that has strong immunosuppressive activity in vivo and prevents the activation of T-lymphocytes in response to antigenic or mitogenic stimulation in vitro. | macrolide lactam | bacterial metabolite; immunosuppressive agent |
N-(2-fluorophenyl)-2-[2-(4-thiazolyl)-1-benzimidazolyl]acetamide | benzimidazoles | ||
biricodar | biricodar: a non-macrocyclic ligand for FKBP12; structure in first source | alpha-amino acid ester | |
l 683590 | immunomycin: from Streptomyces hygroscopicus; structure given in first source | ether; lactol; macrolide; secondary alcohol | antifungal agent; bacterial metabolite; immunosuppressive agent |
cyclosporine | ramihyphin A: one of the metabolites produced by Fusarium sp. S-435; RN given refers to cpd with unknown MF | homodetic cyclic peptide | anti-asthmatic drug; anticoronaviral agent; antifungal agent; antirheumatic drug; carcinogenic agent; dermatologic drug; EC 3.1.3.16 (phosphoprotein phosphatase) inhibitor; geroprotector; immunosuppressive agent; metabolite |
sirolimus | sirolimus : A macrolide lactam isolated from Streptomyces hygroscopicus consisting of a 29-membered ring containing 4 trans double bonds, three of which are conjugated. It is an antibiotic, immunosupressive and antineoplastic agent. Sirolimus: A macrolide compound obtained from Streptomyces hygroscopicus that acts by selectively blocking the transcriptional activation of cytokines thereby inhibiting cytokine production. It is bioactive only when bound to IMMUNOPHILINS. Sirolimus is a potent immunosuppressant and possesses both antifungal and antineoplastic properties. | antibiotic antifungal drug; cyclic acetal; cyclic ketone; ether; macrolide lactam; organic heterotricyclic compound; secondary alcohol | antibacterial drug; anticoronaviral agent; antineoplastic agent; bacterial metabolite; geroprotector; immunosuppressive agent; mTOR inhibitor |
bastadin 5 | |||
timcodar | timcodar: a mutlidrug resistance inhibitor; structure in first source |