Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase. - Wikidata - awgldk - TriplyDB

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

http://www.wikidata.org/entity/Q35127441

about

Dihydrofolate reductase as a model for studies of enzyme dynamics and catalysis Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 A Remote Mutation Affects the Hydride Transfer by Disrupting Concerted Protein Motions in Thymidylate Synthase Mg 2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active Site At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?Effects of macromolecular crowding on protein conformational changes Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complex Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction Preservation of protein dynamics in dihydrofolate reductase evolution Perspective: Defining and quantifying the role of dynamics in enzyme catalysis Effects of Non-Natural Amino Acid Incorporation into the Enzyme Core Region on Enzyme Structure and Function.Computational identification of slow conformational fluctuations in proteins Enzymatic transition states and dynamic motion in barrier crossing.Plastid localization of the key carotenoid enzyme phytoene synthase is altered by isozyme, allelic variation, and activity.How Accurate Are Transition States from Simulations of Enzymatic Reactions?An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.Hydrogen tunneling links protein dynamics to enzyme catalysis Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Single-molecule force spectroscopy approach to enzyme catalysis.Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency Characterizing the dynamics of functionally relevant complexes of formate dehydrogenase.Good vibrations in enzyme-catalysed reactions.Choreographing an enzyme's dance.Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Evolutionary aspects of enzyme dynamics Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors Role of dynamics in enzyme catalysis: substantial versus semantic controversies.Carboxyl-terminal truncations alter the activity of the human α-galactosidase A Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase Comparative laboratory evolution of ordered and disordered enzymes.Survival and risk of relapse of acute lymphoblastic leukemia in a Mexican population is affected by dihydrofolate reductase gene polymorphisms.Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis.Novel non-active site inhibitor of Cryptosporidium hominis TS-DHFR identified by a virtual screen Computational approach for ranking mutant enzymes according to catalytic reaction rates.Experimental evidence for hydrogen tunneling when the isotopic arrhenius prefactor (A(H)/A(D)) is unity.

P2860

Q26766179-D86335D7-9B3B-4225-AB9B-E9E04565F781 Q27320714-1382EF5E-5FF0-4B0E-AAA8-B4EFFEB9AEC4 Q27649699-04B98329-63FF-4A10-8D77-E15B787B2252 Q27674068-FB370DE7-CA6B-4336-95A2-BC256BE4CDA3 Q27677524-23D330AC-3CBB-4F5D-BB52-CF84930EAFE6 Q28271287-5C028E1C-C5F3-48EC-85D9-95DD24E144FC Q28474762-278D9652-6C8C-4E43-9A21-810C370428F9 Q28481478-981715D3-AB6C-4112-8D68-B73FEAED57AA Q28649378-6580EF3D-2204-4ACD-BBDB-CDAC55C6C1DB Q28661130-A3041D21-6DE7-482D-99DD-67CC9FBF5245 Q28834243-9F8DDF27-101A-499B-A5A8-E8DB0A7939BE Q30278633-95047009-C6D7-4EAB-A63C-AC70E18AC50D Q30382464-32C7737E-0AC6-44C4-B0A5-9CF132BBBDA5 Q30494227-5EE597D2-F5BD-4DB8-A49D-AD3F2E9BC54F Q30571334-666826D5-8C0C-47C8-9EE8-1851FE7D437F Q33629992-2E250892-D628-4D24-81DA-A43C53BCE4CD Q33758599-2DC9D11C-3786-46DA-B7BB-390548CB0137 Q33792054-FE53E5AB-EC0C-4511-8773-EEB5B59855F9 Q33794709-D44B356C-D7CE-45A5-B1AA-B17E70743C43 Q33911163-66B458F0-29F1-4AE8-A4A0-459F59791777 Q33917537-1824FC2A-F9DC-4A72-89EB-6D2E280808AF Q33933104-1A2800B3-43A5-45EB-9AD3-B0C130B65DDE Q34241333-4618E0C5-C57D-48F0-9E14-E6F44DC9484E Q34256026-CC95CF01-6DA7-486D-92A0-892AD38BAF7C Q34330740-EE437E57-6E7E-4321-91B4-2B9901CADCE0 Q34408218-3F3E38F0-E446-402D-91F6-DDB15B9307F0 Q34430849-A23E1DFB-1FA8-4945-8D03-3A0C41F69B4D Q35081474-1B4F1AA4-0FCC-4438-95AE-A07835A0746E Q35100667-FD0A35BC-00E3-4FD8-AC37-20DDC6108642 Q35125851-746AEAE7-2A3A-48F8-A129-49B505EC396C Q35127653-8A54BF4B-A7D4-4A03-A6C5-CFC92D459295 Q35194155-1304E19A-F193-4EF4-A7FC-4D964F04DE91 Q35289128-E4F2A4FE-5DEC-4109-8F5E-A71A6F646B99 Q35351471-D8014737-2140-47B5-AA6E-F43C15992A3E Q36224354-530A693B-5899-4DF7-866A-EBE28EB69417 Q36401744-F1BE4037-AB87-4794-B64A-46CCD9265461 Q36924776-12DD929E-B662-4A28-B829-6FB3A584BBCD Q37117303-A3A2ACE4-9CA8-408C-B49C-B330726706D9 Q37148245-5B681875-04F0-4E8C-BB36-789FD73582C1 Q37163630-82C36986-4D54-4210-B314-A2D9CEA5DDC6

P2860

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

http://www.wikidata.org/entity/Q35127441

description

2006 nî lūn-bûn

@nan

2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@ast

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@en

type

label

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@ast

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@en

prefLabel

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@ast

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@en

P1433

Q35127441-D2CDF964-F472-44AB-AA42-11D6873352BC

P1476

Q35127441-3EEC96ED-7C27-4BFC-8188-68C8095BF431

P2093

Q35127441-1E01D5E2-51EF-49DD-A0AE-B52BB474CB66

Q35127441-43133FEA-8B32-4BCD-B503-DA4AEDA84286

Q35127441-4EF0B3B6-A9BF-49E8-99EC-AE2FC03742A8

Q35127441-9485E81D-E23E-4A9A-B22C-0D95D48E5C2B

P2860

Q35127441-0029BF51-E92E-4C11-8EBF-50371281E30A

Q35127441-0A0E15DE-5E2A-4C3F-9AA1-637C839C21B4

Q35127441-1257F90B-A355-4676-BCF0-C14D4DA1E0D8

Q35127441-1BC7B48A-1981-40EC-8E6A-FE043AD84068

Q35127441-219895D3-BA86-4EE0-94DA-D4C195FE33BA

Q35127441-22ED9253-9FC3-4D0B-897F-C4E083E45DC1

Q35127441-25D360CC-6A55-4445-B688-4CAE47E081DB

Q35127441-28D30FC3-5317-441F-B0E2-00E2F8605C9D

Q35127441-28F8ACAE-12FD-4698-9042-15D63B84CE69

Q35127441-2BDA2B3B-C271-4E12-A402-CA50704B6AA8

P304

Q35127441-70D459B5-AC51-4DD7-9FBF-A25263CF422D

P31

Q35127441-1F8AF7AD-3D2C-4F81-9353-D0D85AB088BD

P356

Q35127441-02A59293-6ACF-4126-BE0E-EB04840D3DB5

P407

Q35127441-1EB4FE03-0C76-4C91-9B74-DABA7DBA6297

P433

Q35127441-0DBA2415-87C8-4241-BDBE-93899C636FDE

P478

Q35127441-EE4BEE1E-662C-470A-A9BC-AF294DBD9073

P577

Q35127441-FFA5A4CF-D356-442D-A3D3-099ABD084484

P5875

Q35127441-ABDC9D39-8E1B-468B-B419-D30708E71E12

P698

Q35127441-D034E781-3F04-4244-891B-3341A8B904BE

P932

Q35127441-D9EA6AD7-F06A-4720-82D4-13790DFEE590

P356

PNAS.0606976103

P1433

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

P1476

Coordinated effects of distal ...... ng in dihydrofolate reductase.

@en

P2093

Amnon Kohen

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

Lin Wang

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

Nina M Goodey

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

Stephen J Benkovic

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

P2860

Network of coupled promoting motions in enzyme catalysis

Why bother about clumsiness? The implications of having developmental coordination disorder (DCD)

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes

How enzymes work: analysis by modern rate theory and computer simulations

Electrostatic basis for enzyme catalysis

Evolutionarily conserved networks of residues mediate allosteric communication in proteins

A new conceptual framework for enzyme catalysis

Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.

Linking protein structure and dynamics to catalysis: the role of hydrogen tunnelling.

P304

15753-15758

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

P31

scholarly article

P356

10.1073/PNAS.0606976103

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

P407

P433

43

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

P478

103

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

P577

2006-10-10T00:00:00Z

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

P5875

6762010

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

P698

17032759

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

P932

1635075

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