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2773 14679 Ensembl ENSG00000065135 ENSMUSG00000000001 UniProt P08754 Q9DC51 RefSeq (mRNA) NM_006496 NM_010306 RefSeq (protein) NP_006487 NP_034436 Location (UCSC) Chr 1: 109.55 – 109.6 Mb Chr 3: 108.01 – 108.05 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Guanine nucleotide-binding protein G(k) subunit alpha is a protein that in humans is encoded by the GNAI3 gene ...
The following exergonic equilibrium gives rise to the triiodide ion: . I 2 + I − ⇌ I − 3. In this reaction, iodide is viewed as a Lewis base, and the iodine is a Lewis acid.The process is analogous to the reaction of S 8 with sodium sulfide (which forms polysulfides) except that the higher polyiodides have branched structures.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).
Secondary structure elements: α-helices (red), β-strands (blue arrows). [1] In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, [2] [3] [4] typically in the absence of its macromolecular interaction partners, such as other proteins or RNA.
Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure.