المستودع الأكاديمي جامعة المدينة

Getting specificity from simplicity in putative proteins from the prebiotic Earth

أعرض تسجيلة المادة بشكل مبسط

dc.creator López de la Osa, Jaime
dc.creator Bateman, David A.
dc.creator Ho, Sylvia
dc.creator González, Carlos
dc.creator Chakrabartty, Avijit
dc.creator Laurents, D.V.
dc.date 2008-01-30T17:24:55Z
dc.date 2008-01-30T17:24:55Z
dc.date 2007-09-12
dc.date.accessioned 2017-01-31T00:59:53Z
dc.date.available 2017-01-31T00:59:53Z
dc.identifier Proc Natl Acad Sci U S A. 104(38): 14941–14946 (2007)
dc.identifier 0027-8424
dc.identifier http://hdl.handle.net/10261/2794
dc.identifier 10.1073/pnas.0706876104
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2794
dc.description Can unique protein structures arise from a limited set of amino acids present on the prebiotic Earth? To address this question, we have determined the stability and structure of KIA7, a 20-residue polypeptide containing chiefly Lys, Ile, and Ala. NMR methods reveal that KIA7 tetramerizes and folds on the millisecond time scale to adopt a four-helix X-bundle structure with a tightly and specifically packed core. Denaturation studies and hydrogen exchange measurements of KIA7 and several variants demonstrate that ridges-into-grooves packing of Ala and Ile side chains and the packing of a C-terminal aromatic group into the hydrophobic core are sufficient to give rise to a rather stable, well folded protein structure, with no favorable electrostatic interactions or tertiary or quaternary hydrogen bonds. Both modern proteins and RNAs can adopt specific structures, but RNAs do so with a limited "alphabet" of residues and types of stabilizing interactions. The results reported here show that specific, well folded protein structures can also arise from a highly reduced set of stabilizing interactions and amino acids that are thought to have been present on the prebiotic Earth.
dc.description This work was supported by Spanish Ministry of Science and Education Grant CTQ2004-08275, Alzheimer’s Association Grant NIRG-04-1083, Consejo Superior de Investigaciones Científicas Grant 200580F0131, and a grant from the National Science and Engineering Research Council of Canada.
dc.description Peer reviewed
dc.format 976658 bytes
dc.format application/pdf
dc.language eng
dc.publisher National Academy of Sciences (U.S.)
dc.rights openAccess
dc.subject Four-helix Bundle
dc.subject NMR Spectroscopy
dc.subject Protein Stability
dc.subject Chemical Evolution
dc.subject Protein Folding
dc.title Getting specificity from simplicity in putative proteins from the prebiotic Earth
dc.type Artículo


الملفات في هذه المادة

الملفات الحجم الصيغة عرض

لا توجد أي ملفات مرتبطة بهذه المادة.

هذه المادة تبدو في المجموعات التالية:

أعرض تسجيلة المادة بشكل مبسط