Characterization of Collagen Model Peptides Containing 4-Fluoroproline; (4(S)-Fluoroproline-Pro-Gly)10Forms a Triple Helix, but (4(R)-Fluoroproline-Pro-Gly)10Does Not

2003 ◽  
Vol 125 (33) ◽  
pp. 9922-9923 ◽  
Author(s):  
Masamitsu Doi ◽  
Yoshinori Nishi ◽  
Susumu Uchiyama ◽  
Yuji Nishiuchi ◽  
Takashi Nakazawa ◽  
...  
Keyword(s):  
Triple Helix ◽  
Model Peptides

Synthesis and characterization of new 3′-3′ linked oligodeoxyribonucleotides for alternate strand triple helix formation

Tetrahedron ◽  
1999 ◽  
Vol 55 (32) ◽  
pp. 9899-9914 ◽  
Author(s):  
Lorenzo De Napoli ◽  
Giovanni Di Fabio ◽  
Anna Messere ◽  
Daniela Montesarchio ◽  
Domenica Musumeci ◽  
...  
Keyword(s):  
Triple Helix ◽  
Synthesis And Characterization ◽  
Helix Formation ◽  
Triple Helix Formation

Unambiguous Structure Characterization of a DNA−RNA Triple Helix by15N- and13C-Filtered NOESY Spectroscopy†

Biochemistry ◽  
1996 ◽  
Vol 35 (6) ◽  
pp. 1733-1739 ◽  
Author(s):  
Maria J. P. van Dongen ◽  
Hans A. Heus ◽  
Sybren S. Wymenga ◽  
Gijs A. van der Marel ◽  
Jacques H. van Boom ◽  
...  
Keyword(s):  
Triple Helix ◽  
Structure Characterization ◽  
Rna Triple Helix

scholarly journals Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules

2020 ◽  
Vol 132 (14) ◽  
pp. 5796-5804
Author(s):  
Andreas Maaßen ◽  
Jan M. Gebauer ◽  
Elena Theres Abraham ◽  
Isabelle Grimm ◽  
Jörg‐Martin Neudörfl ◽  
...  
Keyword(s):  
Triple Helix ◽  
Model Peptides

Characterization of the Nucleation Step and Folding of a Collagen Triple-Helix Peptide†

Biochemistry ◽  
2002 ◽  
Vol 41 (25) ◽  
pp. 8143-8151 ◽  
Author(s):  
Yujia Xu ◽  
Manjiri Bhate ◽  
Barbara Brodsky
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix

scholarly journals Characterization of three osteogenesis imperfecta collagen α 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity

1992 ◽  
Vol 288 (1) ◽  
pp. 131-135 ◽  
Author(s):  
J F Bateman ◽  
I Moeller ◽  
M Hannagan ◽  
D Chan ◽  
W G Cole
Keyword(s):  
Osteogenesis Imperfecta ◽  
Triple Helix ◽  
Type I Collagen ◽  
Type I ◽  
Disruptive Effect ◽  
Collagen Triple Helix ◽  
C Terminus ◽  
Glycine Substitution ◽  
C And N

Type I collagen alpha 1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI). The Gly substitutions displayed a gradient of phenotypic severity according to the location of the mutation in the collagen triple helix. The most C-terminal of these, Gly565 to Ser, led to the lethal perinatal (type II) form of OI, whereas the more N-terminal mutations, Gly415 and Gly352 to Ser, led to severe OI (type III/IV) and moderate OI (type IVB) respectively. These data support the notion that glycine substitutions towards the C-terminus of the alpha 1(I) or alpha 2(I) chains will be more clinically severe than those towards the N-terminus. This results from the more disruptive effect of the mutations at the C-terminus on helix initiation and C- and N-terminal helix directional propagation. This generalization must be modified by considering the nature of the glycine substitution and the surrounding amino acid sequence, since the helix is composed of subdomains of differing stability which will affect the ability of helix re-nucleation and propagation.

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