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Daniel Otzen

Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects

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Analysis of protein-protein interactions by mutagenesis : Direct versus indirect effects. / Otzen, Daniel E.; Fersht, Alan R.

In: Protein Engineering, Vol. 12, No. 1, 02.02.1999, p. 41-45.

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Otzen, DE & Fersht, AR 1999, 'Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects', Protein Engineering, vol. 12, no. 1, pp. 41-45.

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Otzen, Daniel E. ; Fersht, Alan R. / Analysis of protein-protein interactions by mutagenesis : Direct versus indirect effects. In: Protein Engineering. 1999 ; Vol. 12, No. 1. pp. 41-45.

Bibtex

@article{c99815f6721147c2a053450e75479e2c,
title = "Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects",
abstract = "Site-directed mutagenesis, including double-mutant cycles, is used routinely for studying protein-protein interactions. We now present a case analysis of chymotrypsin inhibitor 2 (CI2) and subtilisin BPN' using (i) a residue in CI2 that is known to interact directly with subtilisin (Tyr42) and (ii) two CI2 residues that do not have direct contacts with subtilisin (Arg46 and Arg48). We find that there are similar changes in binding energy on mutation of these two sets of residues. It can thus be difficult to interpret mutagenesis data in the absence of structural information.",
keywords = "Chymotrypsin inhibitor 2, Inhibitory activity, Loop flexibility, Protein-protein interactions, Stability, Subtilisin BPN'",
author = "Otzen, {Daniel E.} and Fersht, {Alan R.}",
year = "1999",
month = feb,
day = "2",
language = "English",
volume = "12",
pages = "41--45",
journal = "Protein Engineering Design and Selection (Print)",
issn = "1741-0126",
publisher = "Oxford University Press",
number = "1",

}

RIS

TY - JOUR

T1 - Analysis of protein-protein interactions by mutagenesis

T2 - Direct versus indirect effects

AU - Otzen, Daniel E.

AU - Fersht, Alan R.

PY - 1999/2/2

Y1 - 1999/2/2

N2 - Site-directed mutagenesis, including double-mutant cycles, is used routinely for studying protein-protein interactions. We now present a case analysis of chymotrypsin inhibitor 2 (CI2) and subtilisin BPN' using (i) a residue in CI2 that is known to interact directly with subtilisin (Tyr42) and (ii) two CI2 residues that do not have direct contacts with subtilisin (Arg46 and Arg48). We find that there are similar changes in binding energy on mutation of these two sets of residues. It can thus be difficult to interpret mutagenesis data in the absence of structural information.

AB - Site-directed mutagenesis, including double-mutant cycles, is used routinely for studying protein-protein interactions. We now present a case analysis of chymotrypsin inhibitor 2 (CI2) and subtilisin BPN' using (i) a residue in CI2 that is known to interact directly with subtilisin (Tyr42) and (ii) two CI2 residues that do not have direct contacts with subtilisin (Arg46 and Arg48). We find that there are similar changes in binding energy on mutation of these two sets of residues. It can thus be difficult to interpret mutagenesis data in the absence of structural information.

KW - Chymotrypsin inhibitor 2

KW - Inhibitory activity

KW - Loop flexibility

KW - Protein-protein interactions

KW - Stability

KW - Subtilisin BPN'

UR - http://www.scopus.com/inward/record.url?scp=0033009569&partnerID=8YFLogxK

M3 - Journal article

C2 - 10065709

AN - SCOPUS:0033009569

VL - 12

SP - 41

EP - 45

JO - Protein Engineering Design and Selection (Print)

JF - Protein Engineering Design and Selection (Print)

SN - 1741-0126

IS - 1

ER -