[NMR paper] NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
Related ArticlesNMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
Abstract
All non-fibrillar collagens contain interruptions in the (Gly-X-Y)n repeating sequence, such as the more than 20 interruptions found in chains of basement membrane type IV collagen. Two selectively doubly labeled peptides are designed to model a site in type IV collagen with a GVG interruption in the ?1(IV) and a corresponding GISLK sequence within the ?2(IV) chain. CD and NMR studies on a 2:1 mixture of these two peptides support the formation of a single-component heterotrimer that maintains the one-residue staggering in the triple-helix, has a unique chain register, and contains hydrogen bonds at the interruption site. Formation of hydrogen bonds at interruption sites may provide a driving force for self-assembly and chain register in type IV and other non-fibrillar collagens. This study illustrates the potential role of interruptions in the structure, dynamics, and folding of natural collagen heterotrimers and forms a basis for understanding their biological role.
CD and NMR investigation of collagen peptides mimicking a pathological Gly–Ser mutation and a natural interruption in a similar highly charged sequence context
CD and NMR investigation of collagen peptides mimicking a pathological Gly–Ser mutation and a natural interruption in a similar highly charged sequence context
Abstract
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions while natural interruptions are suggested to play important functional roles. Two peptides—one mimicking a pathological Gly–Ser substitution (ERSEQ) and the other one modeling a similar natural interruption sequence (DRSER)—are designed to facilitate the comparison for elucidating the molecular basis of their different...
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11-27-2015 04:49 PM
[NMR paper] CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
Protein Sci. 2015 Oct 12;
Authors: Sun X, Liu S, Yu W, Wang S, Xiao J
Abstract
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions, while natural interruptions...
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10-13-2015 06:03 PM
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context
ABSTRACT
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions, while natural interruptions are suggested to play important functional roles. Two peptides, one mimicking a pathological Gly-Ser substitution (ERSEQ) and the other one modeling a similar natural interruption sequence (DRSER), are designed to facilitate the comparison for elucidating the molecular basis of their...
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10-13-2015 05:51 AM
Expression, purification and preliminary NMR characterization of isotopically labeled wild-type human heterotrimeric G protein ?i1
Expression, purification and preliminary NMR characterization of isotopically labeled wild-type human heterotrimeric G protein ?i1
August 2012
Publication year: 2012
Source:Protein Expression and Purification, Volume 84, Issue 2</br>
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Molecular-level investigation of proteins is increasingly important to researchers trying to understand the mechanisms of signal transmission. Heterotrimeric G proteins control the activation of many critical signal transmission cascades and are also implicated in numerous diseases. As part of a longer-term investigation of...
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02-03-2013 10:13 AM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
Comparative NMR studies demonstrate profound differences between two viroporins: P7 o
Comparative NMR studies demonstrate profound differences between two viroporins: P7 of HCV and Vpu of HIV-1.
Related Articles Comparative NMR studies demonstrate profound differences between two viroporins: P7 of HCV and Vpu of HIV-1.
Biochim Biophys Acta. 2010 Aug 18;
Authors: Cook GA, Zhang H, Park SH, Wang Y, Opella SJ
The p7 protein from hepatitis C virus and the Vpu protein from HIV-1 are members of the viroporin family of small viral membrane proteins. It is essential to determine their structures in order to obtain an understanding of their...
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08-25-2010 02:04 PM
[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
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[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
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