MOLECULAR MOBILITY IN THE GAP REGIONS OF TYPE-1 COLLAGEN FIBRILS
MOLECULAR MOBILITY IN THE GAP REGIONS OF TYPE-1 COLLAGEN FIBRILS
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DOI：
10.1007/bf01115010
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发表时间：
1986-02-01
影响因子：
4
通讯作者：
TRUS, BL
中科院分区：
文献类型：
--
作者：
FRASER, RDB;TRUS, BL
I型胶原原纤维结构的最近研究（Piez和Trus，Biosci. 1：801-810，1981; Fraser，MacRae，米勒和Suzuki，J. Mol. Biol. Biol.167：497-521，1983）表明，构成差距区的胶原分子片段比构成重叠区的那些片段更具有移动的性。我们分析了两个区域之间的氨基酸残基和三联体类型的分布，发现Ala，Gln，His，Hyp，Leu，Phe和Tyr以及含有两个亚氨基酸残基的三联体的分布显著不均匀。结合差距区域中较低的堆积密度，这些观察结果为理解差距区域中分子链段的更大流动性提供了基础。此外，我们已经检查了两个区域中残基类型的线性分布以及亲水性概况（Kyte和Doolittle，J. Mol. Biol. 157：105-113，1982）。这些揭示了包含螺旋残基165-173、399-407、633-641和867-975的差距区域的区段，其具有最高的亲水指数，不含带电残基，并且含有非常高比例的Ala、Hyp和Phe。
Recent studies of the structure of Type I collagen fibrils (Piez and Trus, Biosci. Rep. 1:801-810, 1981; Fraser, MacRae, Miller and Suzuki, J. Mol. Biol. 167:497-521, 1983) suggest that the segments of the collagen molecule which comprise the gap region are more mobile than those which comprise the overlap region. We have analyzed the distribution of amino acid residues and triplet types between the two regions, and find significantly non-uniform distributions for Ala, Gln, His, Hyp, Leu, Phe, and Tyr, and for triplets containing two imino acid residues. Taken together with the lower packing density in the gap region these observations provide a basis for understanding the greater mobility of the molecular segments in the gap region. In addition, we have examined the linear distribution of residue types in the two regions and also the hydropathy profile (Kyte and Doolittle, J. Mol. Biol. 157:105-113, 1982). These reveal a segment of the gap region comprising helical residues 165-173, 399-407, 633-641 and 867-975 which has the highest hydropathy index, is devoid of charged residues, and contains very high proportions of Ala, Hyp and Phe.