(Q52451866)

1 May 2018

title

Simulation analysis of the stability mutant R96H of T4 lysozyme. (English)

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1 May 2018

2

Karplus M

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1 May 2018

author name string

Tidor B

series ordinal

1

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1 May 2018

language of work or name

English

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publication date

1 April 1991

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1 May 2018

published in

Biochemistry

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1 May 2018

volume

30

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1 May 2018

page(s)

3217-3228

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1 May 2018

issue

13

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1 May 2018

Tinkering with enzymes: what are we learning?

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Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme

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Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein

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Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein

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Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution

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A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof

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Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

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Comparison of the dynamics of myoglobin in different crystal forms

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Mapping protein dynamics by X-ray diffraction

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The alpha-helix dipole and the properties of proteins

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Mutational effects on protein stability

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11 October 2022

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Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00227A009

Identifiers

DOI

10.1021/BI00227A009

1 reference

1 May 2018

PubMed ID

2009262

1 reference

1 May 2018