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Martina Schnölzer

Researcher at Scripps Research Institute

Publications -  11
Citations -  1303

Martina Schnölzer is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Peptide synthesis & Feline immunodeficiency virus. The author has an hindex of 7, co-authored 11 publications receiving 1289 citations.

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Journal ArticleDOI

In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences.

TL;DR: In this paper, simple, effective protocols have been developed for manual and machine-assisted Boc-chemistry solid phase peptide synthesis on polystyrene resins, which use in situ neutralization [i.e. neutralization simultaneous with coupling], high concentrations (> 0.2 M) of Bocamino acid-OBt esters plus base for rapid coupling, 100% TFA for rapid Boc group removal, and a single short (30 s) DMF flow wash between deprotection/coupling and between coupling/deprotection.
Journal ArticleDOI

In Situ Neutralization in Boc-chemistry Solid Phase Peptide Synthesis

TL;DR: The in situ neutralization protocols gave a significant increase in the efficiency of chain assembly, especially for “difficult” sequences arising from sequence-dependent peptide chain aggregation in standard (neutralization prior to coupling) Boc-chemistry SPPS protocols or in Fmoc- chemistry SPPS.
Journal ArticleDOI

Identification of proteolytic processing sites within the Gag and Pol polyproteins of feline immunodeficiency virus.

TL;DR: N-terminal amino acid sequencing, ion spray mass spectrometry, and cleavage of synthetic peptide substrates were used to identify the N and C termini of the mature Gag and Pol proteins of feline immunodeficiency virus.
Journal ArticleDOI

Ion-spray tandem mass spectrometry in peptide synthesis: structural characterization of minor by-products in the synthesis of ACP(65-74).

TL;DR: There was the absence of by-products frequently reported to occur in peptide synthesis, illustrating the high degree of refinement and the accuracy of currently used synthetic methods.
Book ChapterDOI

Synthesis of Proteins by Chemical Ligation of Unprotected Peptide Segments: Mirror-Image Enzyme Molecules, D- & L-HIV Protease Analogs

TL;DR: The 99-residue monomer of the HIV-1 protease molecule was prepared by directed ligation of functionalized unprotected segments by a highly optimized machine-assisted SPPS protocol using Boc-chemistry performed on a modified ABI 430A synthesizer.