Abstract

To test whether the structure of a protein is determined in a manner akin to the assembly of a jigsaw puzzle, up to 10 adjacent residues within the core of T4 lysozyme were replaced by methionine. Such variants are active and fold cooperatively with progressively reduced stability. The structure of a seven-methionine variant has been shown, crystallographically, to be similar to wild type and to maintain a well ordered core. The interaction between the core residues is, therefore, not strictly comparable with the precise spatial complementarity of the pieces of a jigsaw puzzle. Rather, a certain amount of give and take in forming the core structure is permitted. A simplified hydrophobic core sequence, imposed without genetic selection or computer-based design, is sufficient to retain native properties in a globular protein. Study holds ProTherm entries: 1102, 1103, 1104, 1105, 1106, 1107, 1108, 1109, 1110, 1111, 1112, 13518, 13519, 13520, 13521, 13522, 13523, 13524, 13525, 13526, 13527 Extra Details: cysteine-free pseudo wild type lysozyme, 1L63 (C54T, C97A). Activity determined at 20 degree C T4 lysozyme; protein folding; methionine substitutions;,hydrophobic core; stability

Submission Details

ID: 9vu68pzB

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:16 p.m.

Version: 1

Publication Details

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