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Hydrogen-Deuterium Exchange Reveals Catalytically Linked Protein Flexibility in Myoglobin-Mediated Intramolecular C(sp3)-H Activation

ABSTRACT: Hydrogen-Deuterium Exchange Reveals Catalytically Linked Protein Flexibility

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Sickle Cell Disease

SUBMITTER: SHUAIHUA GAO

LAB HEAD: Shuaihua Gao

PROVIDER: PXD071026 | Pride | 2025-12-29

REPOSITORIES: Pride

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			Action	DRS
	Mn_0s_1.raw	Raw
	Mn_1800s_1.raw	Raw
	Mn_300s_1.raw	Raw
	Mn_30s_1.raw	Raw
	Mn_3600s_1.raw	Raw

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Publications

Hydrogen-deuterium exchange reveals catalytically linked protein flexibility in myoglobin-mediated intramolecular C(sp<sup>3</sup>)-H activation.

Gao Hanzi H Camargo Edgar Africano EA Ubi Jude N JN Duan Xiuyuan X Tian Xiaolin X Deng Haiteng H Zheng Guojun G Gao Shuaihua S

Protein science : a publication of the Protein Society 20260101 1

A comprehensive understanding of the biophysical parameters that dictate high catalytic efficiency in enzymes is essential for advancing both fundamental enzymology and its applications. Experimental evidence suggests that protein dynamics play a pivotal role in transiently shaping active site configurations, facilitating the efficient traversal of reaction barriers. In a previous study, protein engineering led to the development of a triple mutant of myoglobin, which enabled the successful synt ...[more]

PMID: 41427743

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