المؤلفون: Sonia Melino, Stefania Di Marco, Alessia Bellomaria, Ridvan Nepravishta, Maurizio Paci

المصدر: Biochemistry. 48:242-253

مصطلحات موضوعية: Secondary, protein synthesis, Amino acid sequences, Peptide, Biochemistry, Consensus sequences, Membrane proteins, genetics, Amines, C-terminal regions, Peptide sequence, chemistry.chemical_classification, zinc, Bacterial, RTN1 protein, Binding properties, Biological functions, Deacetylation, Histone deacetylase, Histone proteins, In-vivo, N terminals, Nervous systems, Spectroscopic techniques, Vesicle trafficking, Acetylation, Amino acids, Binding energy, Nucleic acids, Organic acids, Proteins, Zinc, Biomolecules, histone deacetylase 8, histone H4, membrane protein, nucleic acid, protein RTN1 C, reticulon, unclassified drug, bacterial DNA, bacterial RNA, DNA, nerve protein, protein, RNA, RTN1 protein, human, acetylation, amino acid sequence, article, carboxy terminal sequence, deacetylation, electrophoresis, endoplasmic reticulum, fluorescence, in vivo study, kinetics, membrane vesicle, molecular interaction, priority journal, protein conformation, protein localization, protein protein interaction, regulatory mechanism, sequence homology, binding site, biophysics, chemistry, consensus sequence, Escherichia coli, human, isolation and purification, metabolism, molecular genetics, protein binding, protein motif, protein processing, protein secondary structure, Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Biophysical Processes, Consensus Sequence, DNA, Bacterial, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Conformation, Protein Processing, Post-Translational, Protein Structure, Secondary, RNA, Bacterial, Histone, Protein Structure, Biophysical Phenomena, Consensus sequence, Settore BIO/10, Post-Translational, Reticulon, biology, Nucleic acid structure, Membrane protein, biology.protein, Nucleic acid

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::310567def98ce37fb5106f35caa61e73Test
https://doi.org/10.1021/bi801407wTest

المؤلفون: Stefano Rufini, Sonia Melino, Raffaele Petruzzelli, Maurizio Paci, Marco Sette, Alessandro Grottesi, Roberto D. Morero

المصدر: Biochemistry. 38:9626-9633

مصطلحات موضوعية: Secondary, Circular dichroism, Conformational change, dimethyl sulfoxide, Peptide, Membrane Fusion, Biochemistry, Protein Structure, Secondary, Anti-Infective Agents, alpha helix, protein tertiary structure, Protein secondary structure, chemistry.chemical_classification, conformational transition, histatin, isoprotein, trifluoroethanol, water, zinc ion, amino acid sequence, antimicrobial activity, article, binding site, carboxy terminal sequence, concentration response, metal binding, molecular dynamics, priority journal, protein aggregation, protein binding, protein determination, protein domain, regulatory mechanism, structure analysis, Amino Acid Sequence, Animals, Circular Dichroism, Humans, Liposomes, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Protein Binding, Salivary Proteins, Sequence Analysis, Solutions, Trifluoroethanol, Zinc, Vesicle, Amino acid, Protein Structure, Nuclear Magnetic Resonance, Histatins, Settore BIO/09, Consensus sequence, Settore BIO/10, Salivary Proteins and Peptides, chemistry, Histatin, Biophysics, Biomolecular

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6f9583011fabee0c33d4776d09c2828Test
https://doi.org/10.1021/bi990212cTest