https://forum-sceptique.com/archives/45287.html#45287
"il est impossible de savoir précisément ce qu’il essai de dire." [nouille]
C'est l'article qui "essaie" ("essaie" avec un "E" Juju !) de dire quelque chose mon petit.
DON'T CONFUSE ME WITH THE FACTS !
Certes, comme Bruno l'a mentionné dans un message...
https://forum-sceptique.com/archives/44806.html#44806
...les concepts issus de la théorie de l'évolution permettent d'organiser les connaissances, mais comme l'a mentionné Platecarpus, ils permettent également de préciser le RÔLE des constituants résiduels des protéines en plus de PRÉDIRE et d'identifier leurs sites actifs.
"The evolutionary trace method is a systematic, transparent and novel PREDICTIVE technique that identifies active sites and functional interfaces in proteins with known structure."
J Mol Biol 1996 Mar 29;257(2):342-58
Il s'agit donc d'une amélioration - par rapport à la méthode expérimentale - de la rapidité de détermination des sites fonctionnels (surfaces de liaison) des protéines .Cette amélioration est le résultat direct de l'application de concepts issus de la théorie de l'évolution.
Nous allons maintenant faire bondir la nouille !
L'affirmation de Platecarpus qui déclarait que la biochimie repose sur l'évolution n'est en fait qu'un EUPHÉMISME !
ROFL
Voici pour terminer deux autres articles que le cancre mettra évidemment un point..."d'honneur" (hum !) à comprendre de travers.
Le premier de ces articles est assez récent (février 2003) et ça ne figure peut-être pas encore dans...son...manuel. LOL.
Ah ! Une dernière chose...
IL FAUDRA ÉGALEMENT RÉPONDRE AUX AUTRES QUESTIONS. HMMM ! N'OUBLIE PAS !
J Mol Biol 2003 Feb 7;326(1):255-61
An accurate, sensitive, and scalable method to identify functional sites in protein structures.
Yao H, Kristensen DM, Mihalek I, Sowa ME, Shaw C, Kimmel M, Kavraki L, Lichtarge O.
Department of Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza T921, 77030, Houston, TX, USA
Functional sites determine the activity and interactions of proteins and as such constitute the targets of most drugs. HOWEVER, THE EXPONENTIAL GROWTH OF SEQUENCE AND STRUCTURE DATA FAR EXCEEDS THE ABILITY OF EXPERIMENTAL TECHNIQUES TO IDENTIFY THEIR LOCATIONS AND KEY AMINO ACIDS. To fill this gap we developed a computational Evolutionary Trace method that ranks the evolutionary importance of amino acids in protein sequences. Studies show that the best-ranked residues form fewer and larger structural clusters than expected by chance and overlap with functional sites, but until now the significance of this overlap has remained qualitative. Here, we use 86 diverse protein structures, including 20 determined by the structural genomics initiative, to show that this overlap is a recurrent and statistically significant feature. An automated ET correctly identifies seven of ten functional sites by the least favorable statistical measure, and nine of ten by the most favorable one. THESE RESULTS QUANTITATIVELY DEMONSTRATE THAT A LARGE FRACTION OF FUNCTIONAL SITES IN THE PROTEOME MAY BE ACCURATELY IDENTIFIED FROM SEQUENCE AND STRUCTURE. This should help focus structure-function studies, rational drug design, protein engineering, and functional annotation to the relevant regions of a protein.
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J Mol Biol 1996 Mar 29;257(2):342-58
An evolutionary trace method defines binding surfaces common to protein families.
Lichtarge O, Bourne HR, Cohen FE.
Department of Cellular and Molecular Pharmacology, University of California San Franciso, 94143-0450, USA.
X-ray or NMR structures of proteins are often derived without their ligands, and even when the structure of a full complex is available, the area of contact that is functionally and energetically significant may be a specialized subset of the geometric interface deduced from the spatial proximity between ligands. THUS, EVEN AFTER A STRUCTURE IS SOLVED, IT REMAINS A MAJOR THEORETICAL AND EXPERIMENTAL GOAL TO LOCALIZE PROTEIN FUNCTIONAL INTERFACES AND UNDERSTAND THE ROLE OF THEIR CONSTITUENT RESIDUES. The evolutionary trace method is a systematic, transparent and novel predictive technique that identifies active sites and functional interfaces in proteins with known structure. It is based on the extraction of functionally important residues from sequence conservation patterns in homologous proteins, and on their mapping onto the protein surface to generate clusters identifying functional interfaces. The SH2 and SH3 modular signaling domains and the DNA binding domain of the nuclear hormone receptors provide tests for the accuracy and validity of our method. In each case, the evolutionary trace delineates the functional epitope and identifies residues critical to binding specificity. BASED ON MUTATIONAL EVOLUTIONARY ANALYSIS AND ON THE STRUCTURAL HOMOLOGY OF PROTEIN FAMILIES, this simple and versatile approach should help focus site-directed mutagenesis studies of structure-function relationships in macromolecules, as well as studies of specificity in molecular recognition. More generally, it provides an evolutionary perspective for judging the functional or structural role of each residue in protein structure.
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