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Global Profiling of Lysine Accessibility to Evaluate Protein Structure Changes in Alzheimer’s Disease

ABSTRACT: The linear sequence of amino acids in a protein folds into a 3D structure to execute protein activity and function, but it is still challenging to profile the 3D structure at the proteome scale. Here, we present a method of native protein tandem mass tag (TMT) profiling of Lys accessibility and its application to investigate structural alterations in human brain specimens of Alzheimer’s disease (AD).

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Kaiwen Yu

LAB HEAD: Junmin Peng

PROVIDER: PXD024914 | Pride | 2021-03-23

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Lys_access_f01.pepXML	Pepxml
	Lys_access_f01.raw	Raw
	Lys_access_f02.pepXML	Pepxml
	Lys_access_f02.raw	Raw
	Lys_access_f03.pepXML	Pepxml

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Publications

Global Profiling of Lysine Accessibility to Evaluate Protein Structure Changes in Alzheimer's Disease.

Yu Kaiwen K Niu Mingming M Wang Hong H Li Yuxin Y Wu Zhiping Z Zhang Bin B Haroutunian Vahram V Peng Junmin J

Journal of the American Society for Mass Spectrometry 20210308 4

The linear sequence of amino acids in a protein folds into a 3D structure to execute protein activity and function, but it is still challenging to profile the 3D structure at the proteome scale. Here, we present a method of native protein tandem mass tag (TMT) profiling of Lys accessibility and its application to investigate structural alterations in human brain specimens of Alzheimer's disease (AD). In this method, proteins are extracted under a native condition, labeled by TMT reagents, follow ...[more]

PMID: 33683887

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