Inter-chain proline:proline contacts contribute to the stability of the triple helical conformation.
Inter-chain proline:proline contacts contribute to the stability of the triple helical conformation.
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链间脯氨酸:脯氨酸接触有助于三螺旋构象的稳定性。
DOI:
10.1080/07391102.1988.10507709
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发表时间:
1988
影响因子:
4.4
通讯作者:
Renugopalakrishnan,V
中科院分区:
文献类型:
--
作者:
Bhatnagar,RS;Pattabiraman,N;Sorensen,KR;Langridge,R;MacElroy,RD;Renugopalakrishnan,V
The triple helical conformation observed in the collagen group of proteins is related to the presence of large numbers of imino residues and is derived from the stereochemical properties of these residues. The triple helix is stabilized by increasing numbers of these residues. Hydrogen bonds are usually considered to be a major factor in the formation and stability of protein conformation, however, imino residues are not hydrogen bond donors. We have evaluated the role of these residues in stabilizing the triple helix by re-examining two X-ray based structures of the triple helical polypeptide (Pro-Pro- Gly)10using molecular mechanics calculations. The two minimized structures are comparable in energy and have helical parameters close to the starting values for each starting structure. Our studies suggest that clusters of close van der Waals contacts between proline residues in adjacent chains contribute significantly to the stability of the triple helix. Preliminary NMR studies support this concept. We propose that non-bonded interactions between proline residues may be a significant stabilizing force in the triple helix generated by (Pro-Pro-Gly)10.
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影响因子:
5.6
作者:
B. Olsen;R. Berg;S. Sakakibara;Y. Kishida;D. Prockop
通讯作者:
D. Prockop
DOI:
--
发表时间:
2009
期刊:
International journal of peptide & protein research
影响因子:
--
作者:
R. Rapaka;R. Bhatnagar
通讯作者:
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DOI:
--
发表时间:
1978
期刊:
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通讯作者:
R. Bhatnager
DOI:
--
发表时间:
1968
期刊:
影响因子:
--
作者:
S. Sakakibara;Y. Kishida;Y. Kikuchi;R. Sakai;K. Kakiuchi
通讯作者:
K. Kakiuchi
影响因子:
2.9
作者:
Diem,M;Bhatnagar,RS;Druyan,ME;Renugopalakrishnan,V
通讯作者:
Renugopalakrishnan,V