N-模板化螺旋多肽的大园二色性椭圆率与目前公认的螺旋度算法不一致。
Large Circular Dichroism Ellipticities for N-Templated Helical Polypeptides Are Inconsistent with Currently Accepted Helicity Algorithms.
作者信息
Wallimann Peter, Kennedy Robert J, Kemp Daniel S
机构信息
Department of Chemistry, Rm. 18-582, Massachusetts Institute of Technology, Cambridge, MA 02139 (USA) Fax: (+1) 617-258-7500.
出版信息
Angew Chem Int Ed Engl. 1999 May 3;38(9):1290-1292. doi: 10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E.
Abstract
An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N-templated model peptides of the type AcHel-(Ala Lys) Ala -NH (AcHel-Ala peptide pictured; AcHel is an N-terminal helix-inducing template for polypeptides). These results raise concern over the current methods for determining 100 % helicity.
摘要
通过圆二色光谱法判断，在AcHel-(Ala Lys) Ala -NH这类N模板化模型肽中观察到了前所未有的高度螺旋性（图为AcHel-Ala肽；AcHel是一种用于多肽的N端螺旋诱导模板）。这些结果引发了人们对当前测定100%螺旋性方法的担忧。
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