Rapid, electrostatically assisted association of proteins
The rapid association of barnase and its intracellular inhibitor barstar has been analysed from the effects of mutagenesis and electrostatic screening. A basal association rate constant of 10(5) M(-1) s(-1) is increased to over 5 x 10(9) M(-1) s(-1) by electrostatic forces. The association between the oppositely charged proteins proceeds through the rate-determining formation of an early, weakly specific complex, which is dominated by long-range electrostatic interactions, followed by precise docking to form the high affinity complex. This mode of binding is likely to be used widely in nature to increase association rate constants between molecules and its principles may be used for protein design.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1996 |
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| Erschienen: |
1996 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:3 |
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| Enthalten in: |
Nature structural biology - 3(1996), 5 vom: 17. Mai, Seite 427-31 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Schreiber, G [VerfasserIn] |
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| Themen: |
37328-61-3 |
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| Anmerkungen: |
Date Completed 03.06.1996 Date Revised 23.01.2023 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM085861464 |
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| 245 | 1 | 0 | |a Rapid, electrostatically assisted association of proteins |
| 264 | 1 | |c 1996 | |
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| 500 | |a Date Completed 03.06.1996 | ||
| 500 | |a Date Revised 23.01.2023 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The rapid association of barnase and its intracellular inhibitor barstar has been analysed from the effects of mutagenesis and electrostatic screening. A basal association rate constant of 10(5) M(-1) s(-1) is increased to over 5 x 10(9) M(-1) s(-1) by electrostatic forces. The association between the oppositely charged proteins proceeds through the rate-determining formation of an early, weakly specific complex, which is dominated by long-range electrostatic interactions, followed by precise docking to form the high affinity complex. This mode of binding is likely to be used widely in nature to increase association rate constants between molecules and its principles may be used for protein design | ||
| 650 | 4 | |a Comparative Study | |
| 650 | 4 | |a Journal Article | |
| 650 | 7 | |a Bacterial Proteins |2 NLM | |
| 650 | 7 | |a Enzyme Inhibitors |2 NLM | |
| 650 | 7 | |a barstar protein, Bacillus amyloliquefaciens |2 NLM | |
| 650 | 7 | |a 37328-61-3 |2 NLM | |
| 650 | 7 | |a Ribonucleases |2 NLM | |
| 650 | 7 | |a EC 3.1.- |2 NLM | |
| 650 | 7 | |a Bacillus amyloliquefaciens ribonuclease |2 NLM | |
| 650 | 7 | |a EC 3.1.27.- |2 NLM | |
| 700 | 1 | |a Fersht, A R |e verfasserin |4 aut | |
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