(Q28277014)

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Mapping the transition state and pathway of protein folding by protein engineering

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Mapping the transition state and pathway of protein folding by protein engineering (English)

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A Matouschek

1

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J T Kellis

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2

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L Serrano

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3

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A R Fersht

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4

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language of work or name

English

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publication date

13 July 1989

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published in

Nature

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volume

340

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page(s)

122-6

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issue

6229

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cites work

Toward a better understanding of protein folding pathways

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7 January 2021

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NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli

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Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli

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Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations.

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Mutational analysis of a protein-folding pathway

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Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

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Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis

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Contribution of hydrophobic interactions to protein stability

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Energetics of complementary side-chain packing in a protein hydrophobic core

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Molecular structure of a new family of ribonucleases

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Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization

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Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships

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Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis

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Affinities of amino acid side chains for solvent water

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based on heuristic

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Helix signals in proteins

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Amino acid preferences for specific locations at the ends of alpha helices

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7 January 2021

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Identifiers

DOI

10.1038/340122A0

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Dimensions Publication ID

1010152468

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PubMed ID

2739734

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ResearchGate publication ID

20415970

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Springer Nature article ID

10.1038/340122a0

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(Q28277014)

Mapping the transition state and pathway of protein folding by protein engineering

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