The Experts below are selected from a list of 48 Experts worldwide ranked by ideXlab platform
Hjc Berendsen - One of the best experts on this subject based on the ideXlab platform.
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MOLECULAR-DYNAMICS SIMULATION OF THE STABILITY OF A 22-RESIDUE Alpha-Helix IN WATER AND 30-PERCENT TRIFLUOROETHANOL
Biopolymers, 1993Co-Authors: Ar Vanbuuren, Hjc BerendsenAbstract:A molecular dynamics (MD) simulation was performed on the Alpha-Helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical Right-Handed Alpha-Helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. (C) 1993 John Wiley & Sons, Inc.
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Molecular dynamics simulation of the stability of a 22‐residue α‐helix in water and 30% trifluoroethanol
Biopolymers, 1993Co-Authors: Ar Vanbuuren, Hjc BerendsenAbstract:A molecular dynamics (MD) simulation was performed on the Alpha-Helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical Right-Handed Alpha-Helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. (C) 1993 John Wiley & Sons, Inc.
Mitsuaki Narita - One of the best experts on this subject based on the ideXlab platform.
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Molecular and crystal structures of Aib‐containing oligopeptides Boc‐Leu4‐Aib‐Leu4‐OBzl and Boc‐(Leu4‐Aib)2‐OBzl
Biopolymers, 1991Co-Authors: Kenji Okuyama, Y. Saga, M. Nakayama, Mitsuaki NaritaAbstract:Sample peptides Boc-Leu4-Aib-Leu4-OBzl and Boc-(Leu4-Aib)2-OBzl, were crystallized by the solvent-evaporation method. Both crystals are monoclinic, with space group of P2(1) and Z = 2. The cell parameters are a = 16.580 (7), b = 21.105 (7), c = 11.583 (4) A, and beta = 104.90 (3) degrees (Boc-Leu4-Aib-Leu4-OBzl), and a = 15.247 (9), b = 19.04 (1), c = 16.311 (9) A, and beta = 117.10 (1) degrees [Boc-(Leu4-Aib)2-OBzl]. Crystal structures were solved by the direct method and refined to R values of 0.096 (the former peptide) and 0.112 (the latter). Peptide backbones fold into a Right-Handed Alpha-Helix, except for the C-terminal Aib residue in Boc-(Leu4-Aib)2-OBzl. Both peptide molecules are stabilized by six (the former) or seven (the latter) intramolecular (5----1) hydrogen bonds, and arranged in the head-to-tail fashion, which makes an infinite column. In this column, one (the former) or two (the latter) intermolecular hydrogen bonds link the neighboring molecules. In the case of Boc-Leu4-Aib-Leu4-OBzl, the solvent molecule N,N-dimethylformamide was found in the difference Fourier map. There was a hydrogen bond between peptide and solvent molecule. Along the lateral direction, only hydrophobic contacts were observed between adjacent peptide molecules.
Ar Vanbuuren - One of the best experts on this subject based on the ideXlab platform.
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MOLECULAR-DYNAMICS SIMULATION OF THE STABILITY OF A 22-RESIDUE Alpha-Helix IN WATER AND 30-PERCENT TRIFLUOROETHANOL
Biopolymers, 1993Co-Authors: Ar Vanbuuren, Hjc BerendsenAbstract:A molecular dynamics (MD) simulation was performed on the Alpha-Helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical Right-Handed Alpha-Helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. (C) 1993 John Wiley & Sons, Inc.
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Molecular dynamics simulation of the stability of a 22‐residue α‐helix in water and 30% trifluoroethanol
Biopolymers, 1993Co-Authors: Ar Vanbuuren, Hjc BerendsenAbstract:A molecular dynamics (MD) simulation was performed on the Alpha-Helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical Right-Handed Alpha-Helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. (C) 1993 John Wiley & Sons, Inc.
Kenji Okuyama - One of the best experts on this subject based on the ideXlab platform.
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Molecular and crystal structures of Aib‐containing oligopeptides Boc‐Leu4‐Aib‐Leu4‐OBzl and Boc‐(Leu4‐Aib)2‐OBzl
Biopolymers, 1991Co-Authors: Kenji Okuyama, Y. Saga, M. Nakayama, Mitsuaki NaritaAbstract:Sample peptides Boc-Leu4-Aib-Leu4-OBzl and Boc-(Leu4-Aib)2-OBzl, were crystallized by the solvent-evaporation method. Both crystals are monoclinic, with space group of P2(1) and Z = 2. The cell parameters are a = 16.580 (7), b = 21.105 (7), c = 11.583 (4) A, and beta = 104.90 (3) degrees (Boc-Leu4-Aib-Leu4-OBzl), and a = 15.247 (9), b = 19.04 (1), c = 16.311 (9) A, and beta = 117.10 (1) degrees [Boc-(Leu4-Aib)2-OBzl]. Crystal structures were solved by the direct method and refined to R values of 0.096 (the former peptide) and 0.112 (the latter). Peptide backbones fold into a Right-Handed Alpha-Helix, except for the C-terminal Aib residue in Boc-(Leu4-Aib)2-OBzl. Both peptide molecules are stabilized by six (the former) or seven (the latter) intramolecular (5----1) hydrogen bonds, and arranged in the head-to-tail fashion, which makes an infinite column. In this column, one (the former) or two (the latter) intermolecular hydrogen bonds link the neighboring molecules. In the case of Boc-Leu4-Aib-Leu4-OBzl, the solvent molecule N,N-dimethylformamide was found in the difference Fourier map. There was a hydrogen bond between peptide and solvent molecule. Along the lateral direction, only hydrophobic contacts were observed between adjacent peptide molecules.
M. Nakayama - One of the best experts on this subject based on the ideXlab platform.
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Molecular and crystal structures of Aib‐containing oligopeptides Boc‐Leu4‐Aib‐Leu4‐OBzl and Boc‐(Leu4‐Aib)2‐OBzl
Biopolymers, 1991Co-Authors: Kenji Okuyama, Y. Saga, M. Nakayama, Mitsuaki NaritaAbstract:Sample peptides Boc-Leu4-Aib-Leu4-OBzl and Boc-(Leu4-Aib)2-OBzl, were crystallized by the solvent-evaporation method. Both crystals are monoclinic, with space group of P2(1) and Z = 2. The cell parameters are a = 16.580 (7), b = 21.105 (7), c = 11.583 (4) A, and beta = 104.90 (3) degrees (Boc-Leu4-Aib-Leu4-OBzl), and a = 15.247 (9), b = 19.04 (1), c = 16.311 (9) A, and beta = 117.10 (1) degrees [Boc-(Leu4-Aib)2-OBzl]. Crystal structures were solved by the direct method and refined to R values of 0.096 (the former peptide) and 0.112 (the latter). Peptide backbones fold into a Right-Handed Alpha-Helix, except for the C-terminal Aib residue in Boc-(Leu4-Aib)2-OBzl. Both peptide molecules are stabilized by six (the former) or seven (the latter) intramolecular (5----1) hydrogen bonds, and arranged in the head-to-tail fashion, which makes an infinite column. In this column, one (the former) or two (the latter) intermolecular hydrogen bonds link the neighboring molecules. In the case of Boc-Leu4-Aib-Leu4-OBzl, the solvent molecule N,N-dimethylformamide was found in the difference Fourier map. There was a hydrogen bond between peptide and solvent molecule. Along the lateral direction, only hydrophobic contacts were observed between adjacent peptide molecules.
