Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

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d-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.

P2860

Q33919738-E198D2D7-E5D0-445E-BAAA-97C0768FD699

P2860

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

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http://www.wikidata.org/entity/Q36223944

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@ast

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@en

type

Item

label

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@ast

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@en

prefLabel

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@ast

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@en

P1476

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

@en

P2093

Alexander Gottberg

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

Leela Ruckthong

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

Monika Stachura

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

P2860

Markov state models provide insights into dynamic modulation of protein function

Protein design: toward functional metalloenzymes

Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides

Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coils

Structural Comparisons of Apo- and Metalated Three-Stranded Coiled Coils Clarify Metal Binding Determinants in Thiolate Containing Designed Peptides

Hydrolytic catalysis and structural stabilization in a designed metalloprotein

A Remote Palm Domain Residue of RB69 DNA Polymerase Is Critical for Enzyme Activity and Influences the Conformation of the Active Site

A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins

Water Determines the Structure and Dynamics of Proteins.

Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules.

P304

79-82

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

P31

scholarly article

P356

10.1021/JACS.6B11525

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

P407

English

P433

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

P478

139

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

P50

Lars Hemmingsen

Lorenzo Pecoraro

Saumen Chakraborty

P577

2016-12-14T00:00:00Z

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

P698

27973778

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

P932

5372835

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

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

about

P2860

P2860

Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932