solid phase peptide synthesizer millipore model 9050 plus (Millipore)
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solid phase peptide synthesizer millipore model 9050 plus
Solid Phase Peptide Synthesizer Millipore Model 9050 Plus, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/solid+phase+peptide+synthesizer+millipore+model+9050+plus/automatic+peptide+synthesizer+millipore+9050/pmc02527756-45-10-9
Average 90 stars, based on 1 article reviews
Solid Phase Peptide Synthesizer Millipore Model 9050 Plus, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/solid+phase+peptide+synthesizer+millipore+model+9050+plus/automatic+peptide+synthesizer+millipore+9050/pmc02527756-45-10-9
Average 90 stars, based on 1 article reviews
solid phase peptide synthesizer millipore model 9050 plus - by Bioz Stars,
2026-09
90/100 stars
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other:Article Title: Interaction of Heparin with Two Synthetic Peptides That Neutralize the Anticoagulant Activity of Heparin Article Snippet: L-HIPAP and D-HIPAP were synthesized on a Article Title: Interaction of heparin with two synthetic peptides that neutralize the anticoagulant activity of heparin. Article Snippet: L-HIPAP and D-HIPAP were synthesized on a Article Title: Interaction of Heparin with Two Synthetic Peptides That Neutralize the Anticoagulant Activity of Heparin Article Snippet: Peptide Synthesis L-HIPAP and D-HIPAP were synthesized on a Article Title: Determination of acid dissociation constants of peptide side-chain functional groups by two-dimensional NMR. Article Snippet: An NMR method is described for determining residuespecific acid dissociation constants for peptides which contain more than one residue of the same acidic or basic amino acid.. The method is based on using the differences in CrH proton chemical shifts which result from peptide sequence nearest-neighbor and possibly secondary structure effects to resolve resonances for carbon-bonded reporter protons adjacent to each side-chain acidic group in two-dimensional total correlation spectroscopy (TOCSY) spectra.. Acid dissociation constants were determined for each of the four lysine side-chain ammonium groups of the peptide Lys-Asn-Asn-Gln-Lys-Ser-Glu-Pro-Leu-IleGly-Arg-Lys-Lys-Thr-NH2. |