(Q27677310)

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A mutant T4 lysozyme displays five different crystal conformations

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A mutant T4 lysozyme displays five different crystal conformations (English)

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author name string

H R Faber

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B W Matthews

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language of work or name

English

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publication date

15 November 1990

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published in

Nature

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volume

348

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issue

6298

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page(s)

263-6

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cites work

The Three Dimensional Structure of the Lysozyme from Bacteriophage T4

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7 January 2021

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Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

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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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https://api.crossref.org/works/10.1038%2F348263A0

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7 January 2021

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Structure and thermal stability of phage T4 lysozyme.

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7 January 2021

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Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance

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Protein stability curves

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Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

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7 January 2021

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Structural dynamics of yeast hexokinase during catalysis

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7 January 2021

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Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

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Functional significance of flexibility in proteins

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Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolution

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7 January 2021

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Crystallographic structure studies of an IgG molecule and an Fc fragment

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7 January 2021

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Thermodynamic stability and point mutations of bacteriophage T4 lysozyme

1 reference

stated in

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7 January 2021

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Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins

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Identifiers

DOI

10.1038/348263A0

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Dimensions Publication ID

1013264594

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PubMed publication ID

2234094

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