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A preformed, ordered structure of a 25-residue peptide derived from a major histocompatibility complex class I antigen is required to affect insulin receptor function

Autor: J Stagsted, W A Baase, Avram Goldstein, L Olsson

Publikováno v: Journal of Biological Chemistry. 266:12844-12847

It was recently shown that a 25-residue peptide, Dk-(61-85), derived from the alpha 1 domain of a murine major histocompatibility class I molecule (H-2Dk), affects insulin receptor functions (Hansen, T., Stagsted, J., Pedersen, L., Roth, R. A., Golds

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::21ec0ea2176decd0a7b11615ceb3f92b
https://doi.org/10.1016/s0021-9258(18)98770-3

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Toward a simplification of the protein folding problem: a stabilizing polyalanine .alpha.-helix engineered in T4 lysozyme

Autor: X J Zhang, B W Matthews, W A Baase

Publikováno v: Biochemistry. 30:2012-2017

In an attempt to simplify the protein folding problem, and also to further investigate the role of alanine as a helix-stabilizing residue, a series of alanines was introduced within the alpha-helix that includes residues 126-134 of T4 lysozyme. In wi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46dd4a9d800952a96b20e7d74e60d609
https://doi.org/10.1021/bi00222a001

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Docking molecules by families to increase the diversity of hits in database screens: computational strategy and experimental evaluation

Autor: A I, Su, D M, Lorber, G S, Weston, W A, Baase, B W, Matthews, B K, Shoichet

Publikováno v: Proteins. 42(2)

Molecular docking programs screen chemical databases for novel ligands that fit protein binding sites. When one compound fits the site well, close analogs typically do the same. Therefore, many of the compounds that are found in such screens resemble

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::160584c113874ce0d83198a6e58bfd68
https://pubmed.ncbi.nlm.nih.gov/11119652

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Substitution with selenomethionine can enhance the stability of methionine-rich proteins

Autor: N C, Gassner, W A, Baase, A C, Hausrath, B W, Matthews

Publikováno v: Journal of molecular biology. 294(1)

The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::25c8904655e8fa40bfe6c59881994208
https://pubmed.ncbi.nlm.nih.gov/10556025

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Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability

Autor: J W, Wray, W A, Baase, J D, Lindstrom, L H, Weaver, A R, Poteete, B W, Matthews

Publikováno v: Journal of molecular biology. 292(5)

The mutation Glu108--Val (E108V) in T4 lysozyme was previously isolated as a second-site revertant that specifically compensated for the loss of function associated with the destabilizing substitution Leu99--Gly (L99G). Surprisingly, the two sites ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5c2f94137e507428ea191b3a5818aa5e
https://pubmed.ncbi.nlm.nih.gov/10512706

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Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis

Autor: D W, Heinz, W A, Baase, X J, Zhang, M, Blaber, F W, Dahlquist, B W, Matthews

Publikováno v: Journal of molecular biology. 236(3)

One to four alanines were inserted by site-directed mutagenesis at three different locations within the alpha-helix comprising residues 39 to 50 in bacteriophage T4 lysozyme. All insertion mutants were correctly folded and catalytically active althou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::97b331e114a72fb0a97ae8bb73d97ae5
https://pubmed.ncbi.nlm.nih.gov/8114100

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Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme

Autor: M, Blaber, X J, Zhang, J D, Lindstrom, S D, Pepiot, W A, Baase, B W, Matthews

Publikováno v: Journal of molecular biology. 235(2)

To determine the effects of different amino acids on the structure and stability of an alpha-helix in the context of a globular protein, all 19 naturally-occurring amino acids were substituted for Ser44 in phage T4 lysozyme. A more restricted set of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7ebdaa9f3f7117c6fdde83c953e6ebf4
https://pubmed.ncbi.nlm.nih.gov/8289284

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A preformed, ordered structure of a 25-residue peptide derived from a major histocompatibility complex class I antigen is required to affect insulin receptor function

Autor: J, Stagsted, W A, Baase, A, Goldstein, L, Olsson

Publikováno v: The Journal of biological chemistry. 266(20)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::24c35d3b18ae8e543c034815153e3c5d
https://pubmed.ncbi.nlm.nih.gov/2071573

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Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme

Autor: S, Dao-pin, H, Nicholson, W A, Baase, X J, Zhang, J A, Wozniak, B W, Matthews

Publikováno v: Ciba Foundation symposium. 161

The lysozyme from bacteriophage T4 is being used as a model system to determine the roles of individual amino acids in the folding and stability of a typical globular protein. Such studies can provide quantitative information on the contributions mad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8241b2e5e5955e3e81ee84f187e30bab
https://pubmed.ncbi.nlm.nih.gov/1814696

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