Analysis and design of turns in α-helical hairpins (473 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005; 346(5): 1441-1454.
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Paper type: Journal Article,
Impact factor: 5.229, 5-year impact factor: 3.795
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-13844276055&partnerID=40&md5=6e850486131c8d587b0424911a2abe04
Keywords: Diiron Proteins, Helical Hairpin, Protein Design, Turns, Df1 Protein, Hairpin Protein, Protein Derivative, Unclassified Drug, Alpha Helix, Article, Conformational Transition, Correlation Analysis, Cross Linking, Dimerization, Experimental Design, Molecular Biology, Molecular Interaction, Molecular Model, Nuclear Magnetic Resonance, Priority Journal, Protein Determination, Protein Stability, Sequence Analysis, Structure Analysis, X Ray Crystallography, Amino Acid Sequence, Computational Biology, Computer-Aided Design, X-Ray, Magnetic Resonance Spectroscopy, Metalloproteins, Molecular Sequence Data, Protein Structure, Secondary, Sequence Homology,
Affiliations:
*** IBB - CNR ***
Dept. of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, United States
Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, United States
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
Ctr. Excellence Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy
Department of Protein Design, Centocor, Malvern, PA 19355, United States
Ist. di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Not available.
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005; 346(5): 1441-1454.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.229, 5-year impact factor: 3.795
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-13844276055&partnerID=40&md5=6e850486131c8d587b0424911a2abe04
Keywords: Diiron Proteins, Helical Hairpin, Protein Design, Turns, Df1 Protein, Hairpin Protein, Protein Derivative, Unclassified Drug, Alpha Helix, Article, Conformational Transition, Correlation Analysis, Cross Linking, Dimerization, Experimental Design, Molecular Biology, Molecular Interaction, Molecular Model, Nuclear Magnetic Resonance, Priority Journal, Protein Determination, Protein Stability, Sequence Analysis, Structure Analysis, X Ray Crystallography, Amino Acid Sequence, Computational Biology, Computer-Aided Design, X-Ray, Magnetic Resonance Spectroscopy, Metalloproteins, Molecular Sequence Data, Protein Structure, Secondary, Sequence Homology,
Affiliations:
*** IBB - CNR ***
Dept. of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, United States
Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, United States
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
Ctr. Excellence Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy
Department of Protein Design, Centocor, Malvern, PA 19355, United States
Ist. di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Not available.
Analysis and design of turns in α-helical hairpins
Although the analysis and design of turns that connect the strands in antiparallel β-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an αL-β conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a β-αR-β conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design. © 2004 Elsevier Ltd. All rights reserved.
Although the analysis and design of turns that connect the strands in antiparallel β-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an αL-β conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a β-αR-β conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design. © 2004 Elsevier Ltd. All rights reserved.
Analysis and design of turns in α-helical hairpins
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Analysis and design of turns in α-helical hairpins
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.774
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
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Impact Factor: 12.102
View Export to BibTeX Export to EndNote
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Impact Factor: 2.686
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 5.927
View Export to BibTeX Export to EndNote
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Impact Factor: 5.925
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
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Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Calhoun JR, Nastri F, Maglio O, Pavone V, Lombardi A, Degrado WF
* Artificial diiron proteins: From structure to function (510 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 264-278.
Impact Factor: 2.545
View Export to BibTeX Export to EndNote
Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (385 views)
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Impact Factor: 3.3
View Export to BibTeX Export to EndNote
Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (538 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
View Export to BibTeX Export to EndNote
Maglio O, Nastri F, Pavone V, Lombardi A, Degrado WF
* Preorganization of molecular binding sites in designed diiron proteins (379 views)
P Natl Acad Sci Usa (ISSN: 0027-8424print, 0027-8424linking), 2003 Apr 1; 100(7): 3772-3777.
Impact Factor: 10.272
View Export to BibTeX Export to EndNote
Main ERG, Xiong Y, Cocco MJ, D'Andrea LD, Regan L
* Design of stable α-helical arrays from an idealized TPR motif (1088 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2003; 11(5): 497-508.
Impact Factor: 5.993
View Export to BibTeX Export to EndNote
Pirro F, La Gatta S, Arrigoni F, Famulari A, Maglio O, Vecchio PD, Chiesa M, De Gioia L, Bertini L, Chino M, Nastri F, Lombardi A
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Angewandte Chemie International Edition, 2023/1/2; 62: e202211552-N/D.
Impact Factor: 16.823
View Export to BibTeX Export to EndNote
15 Records (15 excluding Abstracts).
Total impact factor: 89.151 (89.151 excluding Abstracts).
Total 5 year impact factor: 70.848 (70.848 excluding Abstracts).
Total impact factor: 89.151 (89.151 excluding Abstracts).
Total 5 year impact factor: 70.848 (70.848 excluding Abstracts).
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