Evolutionary information for specifying a protein fold (Q28273539)

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Steve W Lockless

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William P Russ

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Heather Lee

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Rama Ranganathan

Understanding protein folding via free-energy surfaces from theory and experiment

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language of work or name

English

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publication date

22 September 2005

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published in

Nature

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volume

437

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issue

7058

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page(s)

512-8

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cites work

1 reference

Ligand-dependent dynamics and intramolecular signaling in a PDZ domain

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The WW domain: a signalling site in dystrophin?

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Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan

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An evolutionary trace method defines binding surfaces common to protein families

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Evolutionarily conserved networks of residues mediate allosteric communication in proteins

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Principles that govern the folding of protein chains

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The present view of the mechanism of protein folding

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Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.

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Co-operative interactions during protein folding.

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Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease

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The linkage between protein folding and functional cooperativity: two sides of the same coin?

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Packing at the protein-water interface

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An analysis of packing in the protein folding problem

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Evolutionarily conserved pathways of energetic connectivity in protein families

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Allosteric determinants in guanine nucleotide-binding proteins

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Structural determinants of allosteric ligand activation in RXR heterodimers.

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Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition

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Statistical coevolution analysis and molecular dynamics: identification of amino acid pairs essential for catalysis

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Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion

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Influence of conservation on calculations of amino acid covariance in multiple sequence alignments

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On evolutionary conservation of thermodynamic coupling in proteins

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Natural-like function in artificial WW domains

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Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.

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WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state

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

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

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Are proteins well-packed?

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Simultaneous determination of protein structure and dynamics.

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A perspective on enzyme catalysis.

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Enzyme dynamics during catalysis

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Myoglobin: the hydrogen atom of biology and a paradigm of complexity

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities

21 January 2018

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van't Hoff enthalpies without baselines.

21 January 2018

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

21 January 2018

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Long-range, small magnitude nonadditivity of mutational effects in proteins

21 January 2018

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

The folding mechanism of a beta-sheet: the WW domain

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03991

inferred from DOI database lookup

7 January 2021

based on heuristic

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03991