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OriginLab corp gaussian curve
NanoESI mass spectrum of gas phase dissociation of protein complex (e.g., holo-myoglobin; apo-myoglobin—heme complex). <t>Gaussian</t> fits of ion intensities of the related charge state series for each molecular or supra-molecular species (complex) are shown (dashed charge state envelope curves). The arrows point to apices which are determined as maxima of fitted curves. The vertical dashed lines provide heights of charge structure envelopes which represent relative intensities of holo-protein complex ions (h, educts; red), ligand ions (i, product; green), and apo-protein ions (j, product; blue). Locations on the m/z axis match with mean charge states of holo-protein complex ions ( m + , educts), ligand ions ( n + , product) as well as apo-protein ions ( p + , product).
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Siepmann GmbH gaussian width
NanoESI mass spectrum of gas phase dissociation of protein complex (e.g., holo-myoglobin; apo-myoglobin—heme complex). <t>Gaussian</t> fits of ion intensities of the related charge state series for each molecular or supra-molecular species (complex) are shown (dashed charge state envelope curves). The arrows point to apices which are determined as maxima of fitted curves. The vertical dashed lines provide heights of charge structure envelopes which represent relative intensities of holo-protein complex ions (h, educts; red), ligand ions (i, product; green), and apo-protein ions (j, product; blue). Locations on the m/z axis match with mean charge states of holo-protein complex ions ( m + , educts), ligand ions ( n + , product) as well as apo-protein ions ( p + , product).
Gaussian Width, supplied by Siepmann GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


NanoESI mass spectrum of gas phase dissociation of protein complex (e.g., holo-myoglobin; apo-myoglobin—heme complex). Gaussian fits of ion intensities of the related charge state series for each molecular or supra-molecular species (complex) are shown (dashed charge state envelope curves). The arrows point to apices which are determined as maxima of fitted curves. The vertical dashed lines provide heights of charge structure envelopes which represent relative intensities of holo-protein complex ions (h, educts; red), ligand ions (i, product; green), and apo-protein ions (j, product; blue). Locations on the m/z axis match with mean charge states of holo-protein complex ions ( m + , educts), ligand ions ( n + , product) as well as apo-protein ions ( p + , product).

Journal: Molecules

Article Title: Mass Spectrometric Analysis of Antibody—Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization

doi: 10.3390/molecules25204776

Figure Lengend Snippet: NanoESI mass spectrum of gas phase dissociation of protein complex (e.g., holo-myoglobin; apo-myoglobin—heme complex). Gaussian fits of ion intensities of the related charge state series for each molecular or supra-molecular species (complex) are shown (dashed charge state envelope curves). The arrows point to apices which are determined as maxima of fitted curves. The vertical dashed lines provide heights of charge structure envelopes which represent relative intensities of holo-protein complex ions (h, educts; red), ligand ions (i, product; green), and apo-protein ions (j, product; blue). Locations on the m/z axis match with mean charge states of holo-protein complex ions ( m + , educts), ligand ions ( n + , product) as well as apo-protein ions ( p + , product).

Article Snippet: Next, these ion intensities were plotted against their respective m/z values and fitted to a Gaussian curve ( ) using Origin version 8.1 (OriginLab Corporation, Northampton, MA, USA).

Techniques: