A review of methods used for identifying structural changes in a large protein complex. - Wikidata - awgldk - TriplyDB

A review of methods used for identifying structural changes in a large protein complex.

A review of methods used for identifying structural changes in a large protein complex.

http://www.wikidata.org/entity/Q37952606

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Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex.Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg(2+).

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A review of methods used for identifying structural changes in a large protein complex.

http://www.wikidata.org/entity/Q37952606

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article científic

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article scientifique

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articol științific

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articolo scientifico

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artigo científico

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artigo científico

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artigo científico

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artikel ilmiah

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A review of methods used for identifying structural changes in a large protein complex.

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A review of methods used for identifying structural changes in a large protein complex.

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A review of methods used for identifying structural changes in a large protein complex.

@en

A review of methods used for identifying structural changes in a large protein complex.

@nl

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A review of methods used for identifying structural changes in a large protein complex.

@en

A review of methods used for identifying structural changes in a large protein complex.

@nl

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978-1-61779-334-9_7

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Methods in Molecular Biology

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A review of methods used for identifying structural changes in a large protein complex.

@en

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Gerald M Carlson

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Owen W Nadeau

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P2860

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure

Structure of proteins: packing of alpha-helices and pleated sheets

Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase

The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin

Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain

The collaboratory for MS3D: a new cyberinfrastructure for the structural elucidation of biological macromolecules and their assemblies using mass spectrometry-based approaches

Finding chimeras: a bioinformatics strategy for identification of cross-linked peptides.

Functional and structural similarities between the inhibitory region of troponin I coded by exon VII and the calmodulin-binding regulatory region of the catalytic subunit of phosphorylase kinase.

Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli.

Single-particle imaging of macromolecules by cryo-electron microscopy.

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117-132

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scholarly article

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10.1007/978-1-61779-334-9_7

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796

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2012-01-01T00:00:00Z

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51769316

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22052488

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3674763

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