Systematic variation of amino acid substitutions for stringent assessment of pairwise covariation (Q56900401)

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3 November 2019

title

Systematic variation of amino acid substitutions for stringent assessment of pairwise covariation (English)

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3 November 2019

6

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3 November 2019

author name string

Sridhar Govindarajan

1

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3 November 2019

Jon E Ness

2

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3 November 2019

Seran Kim

3

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3 November 2019

Emily C Mundorff

4

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3 November 2019

Jeremy Minshull

5

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3 November 2019

language of work or name

English

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publication date

1 May 2003

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Journal of Molecular Biology

3 November 2019

published in

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3 November 2019

volume

328

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3 November 2019

issue

5

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3 November 2019

page(s)

1061-1069

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Predicting functional divergence in protein evolution by site-specific rate shifts

3 November 2019

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Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions

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Function-structure analysis of proteins using covarion-based evolutionary approaches: Elongation factors

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Computational method to reduce the search space for directed protein evolution

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Bona FidePredictions of Protein Secondary Structure Using Transparent Analyses of Multiple Sequence Alignments

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Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently

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DNA shuffling of subgenomic sequences of subtilisin

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Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution

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Molecular recognition at the active site of subtilisin BPN': crystallographic studies using genetically engineered proteinaceous inhibitor SSI (Streptomyces subtilisin inhibitor)

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Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes

7 January 2021

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Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo

7 January 2021

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Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents

7 January 2021

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Growth factor engineering by degenerate homoduplex gene family recombination

7 January 2021

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rtREV: an amino acid substitution matrix for inference of retrovirus and reverse transcriptase phylogeny

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Why are proteins marginally stable?

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Why are proteins so robust to site mutations?

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Different protein sequences can give rise to highly similar folds through different stabilizing interactions.

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Sequence analysis of an artificial family of RNA-binding peptides

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Large libraries reveal diverse solutions to an RNA recognition problem

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Additivity of mutational effects in proteins

7 January 2021

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Exploration of sequence space for protein engineering.

7 January 2021

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High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2

7 January 2021

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Covariance analysis of RNA recognition motifs identifies functionally linked amino acids

7 January 2021

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Covariation of mutations in the V3 loop of human immunodeficiency virus type 1 envelope protein: an information theoretic analysis

7 January 2021

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7 January 2021

Identifiers

DOI

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3 November 2019

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