Stability and function: two constraints in the evolution of barstar and other proteins (Q56903862)

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27 October 2019

title

Stability and function: two constraints in the evolution of barstar and other proteins (English)

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27 October 2019

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2

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27 October 2019

author name string

G Schreiber

series ordinal

1

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27 October 2019

A R Fersht

series ordinal

3

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27 October 2019

language of work or name

English

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publication date

1 October 1994

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27 October 2019

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27 October 2019

volume

2

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27 October 2019

page(s)

945-951

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27 October 2019

issue

10

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Analysis and prediction of the location of catalytic residues in enzymes.

27 October 2019

cites work

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Thermal stability and protein structure

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Mapping the stability determinants of bacterial tyrosyl transfer RNA synthetases by an experimental evolutionary approach

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Strength and co-operativity of contributions of surface salt bridges to protein stability

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Effect of alanine versus glycine in alpha-helices on protein stability

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Dissection of protein structure and folding by directed mutagenesis

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Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability

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7 January 2021

Effect of active site residues in barnase on activity and stability

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Engineering stability of the insulin monomer fold with application to structure-activity relationships

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Affinity maturation of human growth hormone by monovalent phage display

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7 January 2021

Barnase and barstar: two small proteins to fold and fit together

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7 January 2021

Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy

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7 January 2021

Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.

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Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution

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7 January 2021

Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering

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7 January 2021

Kinetics of protein-protein association explained by Brownian dynamics computer simulation

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7 January 2021

Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation

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7 January 2021

Stability of proteins: small globular proteins

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7 January 2021

Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles

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Rational modification of enzyme catalysis by engineering surface charge

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Alpha-helix stability in proteins. II. Factors that influence stability at an internal position

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Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution

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7 January 2021

5'-3' exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis

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7 January 2021

The refolding of cis- and trans-peptidylprolyl isomers of barstar

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7 January 2021

Directed mutagenesis and barnase-barstar recognition.

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7 January 2021

6 Protein engineering in analysis of protein folding pathways and stability

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

10.1016/S0969-2126(94)00096-4

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7866746%20AND%20SRC:MED&resulttype=core&format=json

27 October 2019

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