Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase. - Wikidata - wikimedia - TriplyDB

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

http://www.wikidata.org/entity/Q34721063

about

Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPase.Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation.Why nature really chose phosphate.Identification of β-chain of Fo F1 -ATPase in apoptotic cell population induced by Microplitis bicoloratus bracovirus and its role in the development of Spodoptera litura.Characterization of the thermal and photoinduced reactions of photochromic spiropyrans in aqueous solution.Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F1-ATPase.Molecular Mechanism of ATP Hydrolysis in an ABC Transporter

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P2860

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

http://www.wikidata.org/entity/Q34721063

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

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Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

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Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

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type

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Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

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Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

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Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

@nl

prefLabel

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

@ast

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

@en

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

@en

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Per Lincoln

http://www.w3.org/2001/XMLSchema#string

Tamás Beke-Somfai

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P2860

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase

Direct observation of the rotation of F1-ATPase

On possible pitfalls in ab initio quantum mechanics/molecular mechanics minimization approaches for studies of enzymatic reactions

A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis

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4828-4833

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scholarly article

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12

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108

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