Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site
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چکیده
منابع مشابه
Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site.
Although the cation-pi pair, formed between a side chain or substrate cation and the negative electrostatic potential of a pi system on the face of an aromatic ring, has been widely discussed and has been shown to be important in protein structure and protein-ligand interactions, there has been little discussion of the potential structural and functional importance in proteins of the related an...
متن کاملGround state destabilization from a positioned general base in the ketosteroid isomerase active site.
We compared the binding affinities of ground state analogues for bacterial ketosteroid isomerase (KSI) with a wild-type anionic Asp general base and with uncharged Asn and Ala in the general base position to provide a measure of potential ground state destabilization that could arise from the close juxtaposition of the anionic Asp and hydrophobic steroid in the reaction's Michaelis complex. The...
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Hydrogen bond networks are key elements of biological structure and function. Nevertheless, their structural properties are challenging to assess within complex macromolecules. Hydrogen-bonded protons are not observed in the vast majority of protein X-ray structures, and static crystallographic models provide limited information regarding the dynamical coupling within hydrogen bond networks. We...
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این تحقیق به منظور بررسی رابطه بین میزان استراتژیهای خود-تنظیم شده یادگیری و تمایل به ایجاد ارتباط دانشجویان زبان انگلیسی انجام شده است.علاوه بر این،روابط و کنش های موجود بین ریزسنجه های استراتژیهای خود-تنظیم شده یادگُیری ، مهارت نگارش و تمایل به برقراری ارتباط و همچنین تاٍثیرجنسیت دانشجویان زبان انگلیسی در استراتژیهای خود-تنظیم شده یادگیری و تمایل به برقراری ارتباط آنها مورد بررسی قرار گرفته شد.
15 صفحه اولUncovering the determinants of a highly perturbed tyrosine pKa in the active site of ketosteroid isomerase.
Within the idiosyncratic enzyme active-site environment, side chain and ligand pKa values can be profoundly perturbed relative to their values in aqueous solution. Whereas structural inspection of systems has often attributed perturbed pKa values to dominant contributions from placement near charged groups or within hydrophobic pockets, Tyr57 of a Pseudomonas putida ketosteroid isomerase (KSI) ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2013
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1206710110