(Q27732083)

1

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W A Baase

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F W Dahlquist

3

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B W Matthews

Analysis of insertions/deletions in protein structures

4

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language of work or name

English

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publication date

11 February 1993

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published in

Nature

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volume

361

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issue

6412

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page(s)

561-4

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cites work

1 reference

7 January 2021

Two-codon insertion mutagenesis of plasmid genes by using single-stranded hexameric oligonucleotides

1 reference

7 January 2021

Accommodation of single amino acid insertions by the native state of staphylococcal nuclease

1 reference

7 January 2021

Structural and energetic differences between insertions and substitutions in staphylococcal nuclease.

1 reference

7 January 2021

Consequences of amino acid insertions and/or deletions in transmembrane helix C of bacteriorhodopsin

1 reference

7 January 2021

Insertion of new sequences into the catalytic domain of an enzyme

1 reference

7 January 2021

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

1 reference

7 January 2021

Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

1 reference

7 January 2021

Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins

1 reference

7 January 2021

Loops, bulges, turns and hairpins in proteins

1 reference

7 January 2021

Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme

1 reference

7 January 2021

The interpretation of protein structures: Estimation of static accessibility

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7 January 2021

Solvent-accessible surfaces of proteins and nucleic acids

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7 January 2021

How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins

1 reference

7 January 2021

Helix signals in proteins

1 reference

7 January 2021

Determinants of a protein fold. Unique features of the globin amino acid sequences

1 reference

7 January 2021

A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix

1 reference

7 January 2021

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

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7 January 2021

Protein stability curves

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7 January 2021

Control of enzyme activity by an engineered disulfide bond

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7 January 2021

Rapid and efficient site-specific mutagenesis without phenotypic selection

1 reference

7 January 2021

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

1 reference

7 January 2021

Mutations affecting the lysozyme of phage T4

1 reference

7 January 2021

Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

1 reference

7 January 2021

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

1 reference

7 January 2021