Výsledky vyhledávání - "Laurence A. Angel"

Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes using Ion Mobility-Mass Spectrometry

Autor: Laurence A. Angel, Riccardo Spezia, Charles L. Mitchell, Chloe L. Duvak, Amber A. Flores, Anna V. Arredondo, Anna J. Corrales

Publikováno v: Journal of visualized experiments : JoVE. (184)

This article describes an experimental protocol using electrospray-ion mobility-mass spectrometry (ES-IM-MS) and energy-resolved threshold collision-induced dissociation (TCID) to measure the thermochemistry of the dissociation of negatively-charged

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::663bd749b85f90cdbaf277cb6ecd77e8
https://pubmed.ncbi.nlm.nih.gov/35758714

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Formation of Co(II), Ni(II), Zn(II) complexes of alternative metal binding heptapeptides and nitrilotriacetic acid: Discovering new potential affinity tags

Autor: Nayeli Fuentes, Riccardo Spezia, Ayobami B. Ilesanmi, Oladapo S. Falokun, Linh Truong, Anna V. Arredondo, Amber A. Flores, Laurence A. Angel

Publikováno v: International Journal of Mass Spectrometry
International Journal of Mass Spectrometry, Elsevier, 2021, 463, pp.116554. ⟨10.1016/j.ijms.2021.116554⟩

Using electrospray ionization-ion mobility-mass spectrometry (ESI-IM-MS) a new series of alternative metal binding-5 (amb5) heptapeptides that provide various combinations of His, Cys and Asp as potential metal binding sites are compared for their re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ddfa8cc153d4b05679bad4b144b5abf
https://hal.archives-ouvertes.fr/hal-03162869/file/ambs-affinity-tags_HAL.pdf

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Thermochemical and conformational studies of Ni(II) and Zn(II) ternary complexes of alternative metal binding peptides with nitrilotriacetic acid

Autor: Amber A. Flores, Anna V. Arredondo, Anna J. Corrales, Chloe L. Duvak, Charles L. Mitchell, Oladapo Falokun, Cynthia L. Aguilar, Aram Kim, Bency C. Daniel, H. Derya Karabulut, Riccardo Spezia, Laurence A. Angel

Publikováno v: International Journal of Mass Spectrometry. 473:116792

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::42af7bd0254165be879c67134b8b4804
https://doi.org/10.1016/j.ijms.2021.116792

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Collisional Dynamics Simulations Revealing Fragmentation Properties of Zn(II)-Bound Poly-Peptide

Autor: Abdul Malik, Laurence A. Angel, Riccardo Spezia, William L. Hase

Publikováno v: Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2020, 22 (26), pp.14551-14559. ⟨10.1039/D0CP02463E⟩

Chemical dynamics simulations are performed to study the collision induced gas phase unimolecular fragmentation of a model peptide with the sequence acetyl-His1-Cys2-Gly3-Pro4-Tyr5-His6-Cys7 (analogue methanobactin peptide-5, amb5) and in particular

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc12d506bbe53fd52c74a5fe1cdadf21
https://doi.org/10.26434/chemrxiv.12227336

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Comparison of the pH‐dependent formation of His and Cys heptapeptide complexes of nickel(II), copper(II), and zinc(II) as determined by ion mobility‐mass spectrometry

Autor: Laurence A. Angel, Enas N. Yousef

Publikováno v: Journal of Mass Spectrometry. 55

The analog methanobactin (amb) peptide with the sequence ac-His1 -Cys2 -Gly3 -Pro4 -Tyr5 -His6 -Cys7 (amb5A ) will bind the metal ions of zinc, nickel, and copper. To further understand how amb5A binds these metals, we have undertaken a series of stu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::620b063553ebfa7c8bfef39b34091f22
https://doi.org/10.1002/jms.4489

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ESI-IM-MS reveals the metal binding of three analog methanobactin peptides with different numbers of free Cys at physiological pH

Autor: Rajpal Vangala, Laurence A. Angel

Publikováno v: International Journal of Mass Spectrometry. 468:116640

Three analog methanobactin (amb7) peptides containing the primary structure acetyl-Leu1-His2-Cys3-Gly4-Ser5-Cys6-Tyr7-Pro8-His9-Cys10-Ser11-Cys12-Met13 but differing by the number of disulfide bridges, have been studied for their reactivity with Fe(I

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::95f0f2dc8de520a3a13094a78dcc842c
https://doi.org/10.1016/j.ijms.2021.116640

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Autor: Laurence A. Angel, Ramakrishna Sesham, Enas N. Yousef, Rajpal Vangala, Jacob W. McCabe

Publikováno v: Journal of visualized experiments : JoVE. (151)

Electrospray ionization (ESI) can transfer an aqueous-phase peptide or peptide complex to the gas-phase while conserving its mass, overall charge, metal-binding interactions, and conformational shape. Coupling ESI with ion mobility-mass spectrometry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::088ff6dc01eb7e75e0b69b679a074c84
https://pubmed.ncbi.nlm.nih.gov/31545317

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Direct Dynamics Simulations of Fragmentation of a Zn(II)-2Cys-2His Oligopeptide. Comparison with Mass Spectrometry Collision-Induced Dissociation

Autor: Yu-Fu Lin, Abdul Malik, Laurence A. Angel, William L. Hase, Subha Pratihar

Publikováno v: The journal of physical chemistry. A. 123(32)

Abnormalities in zinc metabolism have been linked to many diseases, including different kinds of cancers and neurological diseases. The present study investigates the fragmentation pathways of a zinc chaperon using a model peptide with the sequence a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35f6cdbe5ad044a66e45c20f368169e9
https://pubmed.ncbi.nlm.nih.gov/31327226

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Weak Acid-Base Interactions of Histidine and Cysteine Affect the Charge States, Tertiary Structure, and Zn(II)-Binding of Heptapeptides

Autor: Cole B. Donald, Yu-Fu Lin, James M. Zahnow, Ying Qin, Linh Truong, Efren Torres, Laurence A. Angel, Enas N. Yousef

Publikováno v: Journal of the American Society for Mass Spectrometry. 30(10)

Zinc fingers are proteins that are characterized by the coordination of zinc ions by an amino acid sequence that commonly contains two histidines and two cysteines (2His-2Cys motif). Investigations of oligopeptides that contain the 2His-2Cys motif, e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::635154680dc7af224c0113119c0ef1ce
https://pubmed.ncbi.nlm.nih.gov/31332742

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