abi 431a solid phase peptide synthesizer (Thermo Fisher)
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abi 431a solid phase peptide synthesizer
Abi 431a Solid Phase Peptide Synthesizer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/peptide+synthesizer+abi+431a/pmc02013942-138-19-17
Average 86 stars, based on 1 article reviews
Abi 431a Solid Phase Peptide Synthesizer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/peptide+synthesizer+abi+431a/pmc02013942-138-19-17
Average 86 stars, based on 1 article reviews
abi 431a solid phase peptide synthesizer - by Bioz Stars,
2026-10
86/100 stars
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Synthesized:Article Title: CONFORMATIONAL FLEXIBILITY AND STRAND ARRANGEMENTS OF THE MEMBRANE-ASSOCIATED HIV FUSION PEPTIDE TRIMER PROBED BY SOLID-STATE NMR SPECTROSCOPY Article Snippet: .. The rest of the trimer was then synthesized using a Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. Article Title: Nuclear Magnetic Resonance Evidence for Retention of a Lamellar Membrane Phase with Curvature in the Presence of Large Quantities of the HIV Fusion Peptide Article Snippet: N -2-hydroxyethylpiperazine- N ′-2-ethanesulfonic acid (HEPES) and Triton X-100 were obtained from Sigma (St. Louis, MO). .. Peptides HFP contained the 23 N-terminal residues of HIV gp41 (AVGIGALFLGFLGAAGSTMGARS) and was synthesized as a C-terminal amide using a Article Title: Oligomeric β -Structure of the Membrane-Bound HIV-1 Fusion Peptide Formed from Soluble Monomers Article Snippet: .. All peptides were synthesized as their C-terminal amides using a Article Title: Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples. Article Snippet: The human immunodeficiency virus (HIV) and influenza virus fusion peptides are ∼20-residue sequences which catalyze the fusion of viral and host cell membranes.. The orientations of these peptides in lipid bilayers have been probed with 15N solid-state nuclear magnetic resonance (NMR) spectroscopy of samples containing membranes oriented between stacked glass plates.. Each of the peptides adopts at least two distinct conformations in membranes (predominantly helical or beta strand) and the conformational distribution is determined in part by the membrane headgroup and cholesterol composition. Article Title: Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide. Article Snippet: N-2-hydroxyethylpiperazine-N′2-ethanesulfonic acid (HEPES) and Triton X-100 were obtained from Sigma (St. Louis, MO). .. HFP contained the 23 N-terminal residues of HIV gp41 (AVGIGALFLGFLGAAGSTMGARS) and was synthesized as a C-terminal amide using a Molecular Weight:Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. Analysis:Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. Analytical Ultracentrifugation:Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. Sequencing:Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. Solubility:Article Title: 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations. Article Snippet: and correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner, Charles M. Gabrys, Jochem O. Struppe, and David P. Weliky, Citation: The Journal of Chemical Physics 128, 052319 (2008); doi: 10.1063/1.2829984 View online: http://dx.doi.org/10.1063/1.2829984 View Table of Contents: http://aip.scitation.org/toc/jcp/128/5 Published by the American Institute of Physics 13C– 13C and 15N– 13C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations Michele L. Bodner,1 Charles M. Gabrys,1 Jochem O. Struppe,2 and David P. Weliky1,a 1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA 2Bruker Biospin Corporation, NMR Division, Billerica, Massachusetts 01821, USA Received 29 October 2007; accepted 6 December 2007; published online 4 February 2008 Many viruses which cause disease including human immunodeficiency virus HIV and influenza are “enveloped” by a membrane and infection of a host cell begins with joining or “fusion” of the viral and target cell membranes.. Fusion is catalyzed by viral proteins in the viral membrane.. For HIV and for the influenza virus, these fusion proteins contain an 20-residue apolar “fusion peptide” that binds to target cell membranes and plays a critical role in fusion. other:Article Title: Fibrillin-1 and fibrillin-2 show temporal and tissue-specific regulation of expression in developing elastic tissues. Article Snippet: 'Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri; *Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, New York; §School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania; "Department of Pathology, University of Adelaide, Adelaide, Australia; "Dermatology and 'Respiratory and Critical Care Divisions, Department of Medicine, Jewish Hospital at Washington University School of Medicine, St. Louis, Missouri Article Title: Synthetic, site-specific biotinylated analogs of human MCP-1. Article Snippet: Human monocyte chemoattractant protein 1 (MCP-1, CCL2) is a 8.6-kDa protein that has been implicated in a number of diseases including atherosclerosis, rheumatoid arthritis, chronic obstructive pulmonary disease and cancer.. As part of a program to identify antibodies against MCP-1, we synthesized site-specific, biotinylated human MCP-1 analogs to be used for panning of an antibody phage display library.. In contrast to material obtained from random biotinylation, the site-specific biotinylated analogs were homogeneous and retained full activity. Purification:Article Title: Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples. Article Snippet: The human immunodeficiency virus (HIV) and influenza virus fusion peptides are ∼20-residue sequences which catalyze the fusion of viral and host cell membranes.. The orientations of these peptides in lipid bilayers have been probed with 15N solid-state nuclear magnetic resonance (NMR) spectroscopy of samples containing membranes oriented between stacked glass plates.. Each of the peptides adopts at least two distinct conformations in membranes (predominantly helical or beta strand) and the conformational distribution is determined in part by the membrane headgroup and cholesterol composition. High Performance Liquid Chromatography:Article Title: Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples. Article Snippet: The human immunodeficiency virus (HIV) and influenza virus fusion peptides are ∼20-residue sequences which catalyze the fusion of viral and host cell membranes.. The orientations of these peptides in lipid bilayers have been probed with 15N solid-state nuclear magnetic resonance (NMR) spectroscopy of samples containing membranes oriented between stacked glass plates.. Each of the peptides adopts at least two distinct conformations in membranes (predominantly helical or beta strand) and the conformational distribution is determined in part by the membrane headgroup and cholesterol composition. |