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  2. Kickers, Inc. - Wikipedia

    en.wikipedia.org/wiki/Kickers,_Inc.

    Kickers, Inc. is a twelve-issue comic book series published by Marvel Comics from 1986 to 1987 as part of the New Universe imprint. Created by Tom DeFalco and Ron Frenz, the series featured a group of former professional American football players for the fictional New York Smashers team who became a group of heroes for hire, calling themselves "Kickers Inc."

  3. Levinthal's paradox - Wikipedia

    en.wikipedia.org/wiki/Levinthal's_paradox

    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 ...

  4. Small protein - Wikipedia

    en.wikipedia.org/wiki/Small_protein

    Small proteins are a diverse fold class of proteins (usually <100 amino acids long). [ 1 ][ 2 ][ 3 ] Their tertiary structure is usually maintained by disulphide bridges, [ 4 ] metal ligands, [ 5 ] and or cofactors such as heme. Some small proteins serve important regulatory functions by direct interaction with certain enzymes and are therefore ...

  5. Gregory L. Verdine - Wikipedia

    en.wikipedia.org/wiki/Gregory_L._Verdine

    Gregory L. Verdine (born June 10, 1959) is an American chemical biologist, biotech entrepreneur, venture capitalist and university professor. [3] He is a founder of the field of chemical biology, [citation needed] which deals with the application of chemical techniques to biological systems. His work has focused on mechanisms of DNA repair and ...

  6. Cystine knot - Wikipedia

    en.wikipedia.org/wiki/Cystine_knot

    A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The sections of polypeptide that occur between two of them form a loop through which a third disulfide bond passes, forming a rotaxane substructure. The cystine knot motif stabilizes protein structure and is conserved in ...

  7. Cysteine-rich protein - Wikipedia

    en.wikipedia.org/wiki/Cysteine-rich_protein

    Cysteine-rich proteins (CRP, cysteine-rich peptide or disulphide-rich peptide) are small proteins that contain a large number of cysteines. These cysteines either cross-link to form disulphide bonds, or bind metal ions by chelation, stabilising the protein's tertiary structure. [1][2][3] CRPs include a highly conserved secretion peptide signal ...

  8. Gary Ruvkun - Wikipedia

    en.wikipedia.org/wiki/Gary_Ruvkun

    The molecular genetic analysis of symbiotic nitrogen fixation (NIF) genes from rhizobium meliloti (1982) Doctoral advisor. Frederick Ausubel. Website. ruvkun.hms.harvard.edu. Gary Bruce Ruvkun (born March 26, 1952) is an American molecular biologist and Nobel laureate at Massachusetts General Hospital and professor of genetics at Harvard ...

  9. Leucine zipper - Wikipedia

    en.wikipedia.org/wiki/Leucine_zipper

    Leucine zipper. "Overhead view", or helical wheel diagram, of a leucine zipper, where d represents leucine, arranged with other amino acids on two parallel alpha helices. A leucine zipper (or leucine scissors[1]) is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 [2 ...