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2007年の論文 מאמר מדעי bilimsel makale artigo científico artículu científicu 2007年學術文章 2007年学术文章 scienca artikolo наукова стаття, опублікована в жовтні 2007 teaduslik artikkel naučni članak wetenschappelijk artikel videnskabelig artikel ৯ অক্টোবর ২০০৭-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ artigo científico vitenskapelig artikkel 2007년 논문 2007年学术文章 vedecký článok სამეცნიერო სტატია научна статия 2007年學術文章 научни чланак wissenschaftlicher Artikel articol științific artikel ilmiah artikull shkencor 2007年學術文章 мақолаи илмӣ مقالة علمية نشرت في 9 أكتوبر 2007 2007年學術文章 2007年学术文章 vědecký článek tudományos cikk artigo científico artículo científico publicado en 2007 article científic vitskapeleg artikkel 2007年学术文章 บทความทางวิทยาศาสตร์ artykuł naukowy tieteellinen artikkeli 2007 թվականի հոկտեմբերի 9-ին հրատարակված գիտական հոդված επιστημονικό άρθρο научная статья scientific article published on 9 October 2007 article scientific artikulong pang-agham scientific article published on 9 October 2007 2007 nî lūn-bûn article scientifique 2007年学术文章 2007年学术文章 articolo scientifico vetenskaplig artikel научни чланак bài báo khoa học 2007年學術文章 scientific article published on 9 October 2007
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Humeyra Taskent Konstantinos N Aprilakis
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Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
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Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
schema:name
Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
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Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
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10.1021/BI7010674