(Q30353521)

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Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.

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Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. (English)

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Karplus M

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2

Petsko GA

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Joseph D

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2402636

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English

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1 September 1990

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249

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4975

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1425-1428

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Structural domains in proteins and their role in the dynamics of protein function

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Structure of yeast triosephosphate isomerase at 1.9-A resolution

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.2402636

Dynamics of folded proteins

1 reference

11 October 2022

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Active site dynamics in protein molecules: a stochastic boundary molecular-dynamics approach.

1 reference

11 October 2022

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The hinge-bending mode in lysozyme

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Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.

1 reference

11 October 2022

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Molecular dynamics simulations of "loop closing" in the enzyme triose phosphate isomerase

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11 October 2022

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Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison

1 reference

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

1 reference

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Hydrogen bonding in globular proteins

1 reference

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Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?

1 reference

11 October 2022

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10.1126/SCIENCE.2402636

1 reference

stated in

Europe PubMed Central

20 June 2017

1 reference

Europe PubMed Central

PubMed ID

2402636

retrieved

20 June 2017

(Q30353521)

Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.

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