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  2. Bacteriorhodopsin - Wikipedia

    en.wikipedia.org/wiki/Bacteriorhodopsin

    Bacteriorhodopsin (Bop) is a protein used by Archaea, most notably by haloarchaea, a class of the Euryarchaeota. [1] It acts as a proton pump; that is, it captures light energy and uses it to move protons across the membrane out of the cell. [2] The resulting proton gradient is subsequently converted into chemical energy. [3]

  3. Catenin beta-1 - Wikipedia

    en.wikipedia.org/wiki/Catenin_beta-1

    [5] [6] In Drosophila, the homologous protein is called armadillo. β-catenin is a subunit of the cadherin protein complex and acts as an intracellular signal transducer in the Wnt signaling pathway. [ 7 ] [ 8 ] [ 9 ] It is a member of the catenin protein family and homologous to γ-catenin , also known as plakoglobin . β-Catenin is widely ...

  4. Aquaporin - Wikipedia

    en.wikipedia.org/wiki/Aquaporin

    In 1999, together with other research teams, Agre reported the first high-resolution images of the three-dimensional structure of an aquaporin, namely, aquaporin-1. [23] Further studies using supercomputer simulations identified the pathway of water as it moved through the channel and demonstrated how a pore can allow water to pass without the ...

  5. Hibernation factor - Wikipedia

    en.wikipedia.org/wiki/Hibernation_factor

    Balon (Spanish "ball", after homologue Pelota) [5] is a hibernation factor protein found in the cold-adapted bacterium Psychrobacter urativorans. [5] The protein was discovered accidentally by a researcher who unintentionally left a sample of P. urativorans in an ice bucket for too long, cold-shocking it, through subsequent cryo-EM scans of the ...

  6. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    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).

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding must be thermodynamically favorable within a cell in order for it to be a spontaneous reaction. Since it is known that protein folding is a spontaneous reaction, then it must assume a negative Gibbs free energy value. Gibbs free energy in protein folding is directly related to enthalpy and entropy. [12]

  8. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids are not typical component of food: animals eat proteins. The protein is broken down into amino acids in the process of digestion. They are then used to synthesize new proteins, other biomolecules, or are oxidized to urea and carbon dioxide as a source of energy. [78]

  9. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...