41
switch: application to Thermoanaerobacter
tengcongensis
ribose
binding
protein.
Biochemistry 52(4):600–612. doi:10.1021/
bi301105u
5. Graf R, Schachman HK (1996) Random circular permutation of genes and expressed
polypeptide chains: application of the method
to the catalytic chains of aspartate transcarbamoylase. Proc Natl Acad Sci U S A
93(21):11591–11596
6. Hennecke J, Sebbel P, Glockshuber R (1999)
Random circular permutation of DsbA reveals
segments that are essential for protein folding
and stability. J Mol Biol 286(4):1197–1215.
doi:10.1006/jmbi.1998.2531
7. Iwakura M, Nakamura T, Yamane C, Maki K
(2000) Systematic circular permutation of
an entire protein reveals essential folding
elements. Nat Struct Biol 7(7):580–585.
doi:10.1038/76811
8. Qian Z, Lutz S (2005) Improving the catalytic
activity of Candida antarctica lipase B by circular
permutation. J Am Chem Soc 127(39):13466–
13467. doi:10.1021/ja053932h
9. Reitinger S, Yu Y, Wicki J, Ludwiczek M,
D’Angelo I, Baturin S, Okon M, Strynadka NC,
Lutz S, Withers SG, McIntosh LP (2010)
Circular permutation of Bacillus circulans xylanase: a kinetic and structural study. Biochemistry
49(11):2464–2474. doi:10.1021/bi100036f
10. Carlson HJ, Cotton DW, Campbell RE (2010)
Circularly permuted monomeric red fluorescent proteins with new termini in the betasheet.
Protein
Sci
19(8):1490–1499.
doi:10.1002/pro.428
11. Guntas G, Mansell TJ, Kim JR, Ostermeier
M (2005) Directed evolution of protein
switches and their application to the creation of ligand- binding proteins. Proc Natl
Acad Sci U S A 102(32):11224–11229.
doi:10.1073/pnas.0502673102
12. Iwakura M, Nakamura T (1998) Effects of the
length of a glycine linker connecting the N-and
C-termini of a circularly permuted dihydrofolate reductase. Protein Eng 11(8):707–713
13. Flores G, Soberon X, Osuna J (2004) Production
of a fully functional, permuted single- chain penicillin G acylase. Protein Sci 13(6):1677–1683.
doi:10.1110/ps.03436604
14. Qian Z, Horton JR, Cheng X, Lutz S (2009)
Structural redesign of lipase B from Candida
antarctica by circular permutation and incremental truncation. J Mol Biol 393(1):191–
201. doi:10.1016/j.jmb.2009.08.008
15. Correia BE, Holmes MA, Huang PS, Strong
RK, Schief WR (2011) High-resolution structure prediction of a circular permutation loop.
Protein Sci 20(11):1929–1934. doi:10.1002/
pro.725
16. Butler JS, Mitrea DM, Mitrousis G, Cingolani
G, Loh SN (2009) Structural and thermodynamic analysis of a conformationally strained
circular permutant of barnase. Biochemistry
48(15):3497–3507. doi:10.1021/bi900039e
17. Grimsley GR, Trevino SR, Thurlkill RL, Scholtz
JM (2013) Determining the conformational
stability of a protein from urea and thermal
unfolding curves. Curr Protoc Protein Sci .
doi:10.1002/0471140864.ps2804s71Chapter
28:Unit28 24
18. Ho SN, Hunt HD, Horton RM, Pullen JK,
Pease LR (1989) Site-directed mutagenesis by
overlap extension using the polymerase chain
reaction. Gene 77:51–59
Engineering Allosteric Protein Switches
switch: application to Thermoanaerobacter
tengcongensis
ribose
binding
protein.
Biochemistry 52(4):600–612. doi:10.1021/
bi301105u
5. Graf R, Schachman HK (1996) Random circular permutation of genes and expressed
polypeptide chains: application of the method
to the catalytic chains of aspartate transcarbamoylase. Proc Natl Acad Sci U S A
93(21):11591–11596
6. Hennecke J, Sebbel P, Glockshuber R (1999)
Random circular permutation of DsbA reveals
segments that are essential for protein folding
and stability. J Mol Biol 286(4):1197–1215.
doi:10.1006/jmbi.1998.2531
7. Iwakura M, Nakamura T, Yamane C, Maki K
(2000) Systematic circular permutation of
an entire protein reveals essential folding
elements. Nat Struct Biol 7(7):580–585.
doi:10.1038/76811
8. Qian Z, Lutz S (2005) Improving the catalytic
activity of Candida antarctica lipase B by circular
permutation. J Am Chem Soc 127(39):13466–
13467. doi:10.1021/ja053932h
9. Reitinger S, Yu Y, Wicki J, Ludwiczek M,
D’Angelo I, Baturin S, Okon M, Strynadka NC,
Lutz S, Withers SG, McIntosh LP (2010)
Circular permutation of Bacillus circulans xylanase: a kinetic and structural study. Biochemistry
49(11):2464–2474. doi:10.1021/bi100036f
10. Carlson HJ, Cotton DW, Campbell RE (2010)
Circularly permuted monomeric red fluorescent proteins with new termini in the betasheet.
Protein
Sci
19(8):1490–1499.
doi:10.1002/pro.428
11. Guntas G, Mansell TJ, Kim JR, Ostermeier
M (2005) Directed evolution of protein
switches and their application to the creation of ligand- binding proteins. Proc Natl
Acad Sci U S A 102(32):11224–11229.
doi:10.1073/pnas.0502673102
12. Iwakura M, Nakamura T (1998) Effects of the
length of a glycine linker connecting the N-and
C-termini of a circularly permuted dihydrofolate reductase. Protein Eng 11(8):707–713
13. Flores G, Soberon X, Osuna J (2004) Production
of a fully functional, permuted single- chain penicillin G acylase. Protein Sci 13(6):1677–1683.
doi:10.1110/ps.03436604
14. Qian Z, Horton JR, Cheng X, Lutz S (2009)
Structural redesign of lipase B from Candida
antarctica by circular permutation and incremental truncation. J Mol Biol 393(1):191–
201. doi:10.1016/j.jmb.2009.08.008
15. Correia BE, Holmes MA, Huang PS, Strong
RK, Schief WR (2011) High-resolution structure prediction of a circular permutation loop.
Protein Sci 20(11):1929–1934. doi:10.1002/
pro.725
16. Butler JS, Mitrea DM, Mitrousis G, Cingolani
G, Loh SN (2009) Structural and thermodynamic analysis of a conformationally strained
circular permutant of barnase. Biochemistry
48(15):3497–3507. doi:10.1021/bi900039e
17. Grimsley GR, Trevino SR, Thurlkill RL, Scholtz
JM (2013) Determining the conformational
stability of a protein from urea and thermal
unfolding curves. Curr Protoc Protein Sci .
doi:10.1002/0471140864.ps2804s71Chapter
28:Unit28 24
18. Ho SN, Hunt HD, Horton RM, Pullen JK,
Pease LR (1989) Site-directed mutagenesis by
overlap extension using the polymerase chain
reaction. Gene 77:51–59
Engineering Allosteric Protein Switches