NUCLEATION, RAPID FOLDING, AND GLOBULAR INTRACHAIN REGIONS IN PROTEINS
NUCLEATION, RAPID FOLDING, AND GLOBULAR INTRACHAIN REGIONS IN PROTEINS
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DOI：
10.1073/pnas.70.3.697
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发表时间：
1973-01-01
影响因子：
11.1
通讯作者：
WETLAUFE.DB
中科院分区：
文献类型：
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作者：
WETLAUFE.DB
在一些由单多肽链组成的球状蛋白中发现了不同的结构区域。这些区域的存在和肽链在其中的连续性，再加上动力学参数，表明三维结构形成（成核）的早期阶段独立发生在这些分子的不同部分。通过添加氨基酸序列中靠近细胞核的肽链片段，细胞核可以快速生长。这样的过程将产生三维（天然）蛋白质结构，其中包含连续肽链的分离区域。讨论了检验这一假设的可能方法。
Distinct structural regions have been found in several globular proteins composed of single polypeptide chains. The existence of such regions and the continuity of peptide chain within them, coupled with kinetic arguments, suggests that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules. A nucleus can grow rapidly by adding peptide chain segments that are close to the nucleus in aminoacid sequence. Such a process would generate three-dimensional (native) protein structures that contain separate regions of continuous peptide chain. Possible means of testing this hypothesis are discussed.