A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis (Q27640188)

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15 December 2019

title

A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis (English)

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15 December 2019

3

Brian W Matthews

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15 December 2019

author name string

Xue-jun Zhang

series ordinal

1

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15 December 2019

Walter A Baase

series ordinal

2

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15 December 2019

publication date

1 December 2002

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15 December 2019

published in

Biophysical Chemistry

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15 December 2019

volume

101-102

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15 December 2019

page(s)

43-56

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The Three Dimensional Structure of the Lysozyme from Bacteriophage T4

15 December 2019

cites work

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Comparison of the predicted and observed secondary structure of T4 phage lysozyme

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A test of proposed rules for helix capping: Implications for protein design

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Phage T4 lysozyme Physical properties and reversible unfolding

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Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes

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Stability of phage T4 lysozymes. II. Unfolding with guanidinium chloride

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Mutations and protein stability

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Thermodynamic stability and point mutations of bacteriophage T4 lysozyme

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Thermal denaturation of bacteriophage T4 lysozyme at neutral pH.

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Characterizing transition states in protein folding: an essential step in the puzzle

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Sequence determinants of folding and stability for the P22 Arc repressor dimer.

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High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis

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Deciphering the message in protein sequences: tolerance to amino acid substitutions

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Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme

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Protein stability effects of a complete set of alanine substitutions in Arc repressor

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Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis

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Tolerance of Arc repressor to multiple-alanine substitutions

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7 January 2021

Multiple alanine replacements within α‐helix 126–134 of T4 lysozyme have independent, additive effects on both structure and stability

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Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence

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Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent

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Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Control of enzyme activity by an engineered disulfide bond

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Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft

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Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme

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7 January 2021

Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme

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7 January 2021

The detection of sub-units within the crystallographic asymmetric unit

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Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

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Beta-turns and their distortions: a proposed new nomenclature

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Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C

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7 January 2021

A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme

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7 January 2021

The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.

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Helix signals in proteins

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Capping and alpha-helix stability

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Identifiers

DOI

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15 December 2019

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