![Main Chain Hydrogen Bond Interactions in the Binding of Proline-rich Gluten Peptides to the Celiac Disease-associated HLA-DQ2 Molecule - ScienceDirect Main Chain Hydrogen Bond Interactions in the Binding of Proline-rich Gluten Peptides to the Celiac Disease-associated HLA-DQ2 Molecule - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0021925820691190-gr1.jpg)
Main Chain Hydrogen Bond Interactions in the Binding of Proline-rich Gluten Peptides to the Celiac Disease-associated HLA-DQ2 Molecule - ScienceDirect
Enantiopure 5-CF3–Proline: Synthesis, Incorporation in Peptides, and Tuning of the Peptide Bond Geometry | Organic Letters
![Peptidyl-prolyl isomerisation. Cis/trans isomerisation of the peptide... | Download Scientific Diagram Peptidyl-prolyl isomerisation. Cis/trans isomerisation of the peptide... | Download Scientific Diagram](https://www.researchgate.net/publication/11320521/figure/fig1/AS:431972787986433@1480001746888/Peptidyl-prolyl-isomerisation-Cis-trans-isomerisation-of-the-peptide-bond-arrow.png)
Peptidyl-prolyl isomerisation. Cis/trans isomerisation of the peptide... | Download Scientific Diagram
![Amino acid sequence constituting the primary structure of collagen C 12... | Download Scientific Diagram Amino acid sequence constituting the primary structure of collagen C 12... | Download Scientific Diagram](https://www.researchgate.net/publication/8207830/figure/fig1/AS:349357284053009@1460304675884/Amino-acid-sequence-constituting-the-primary-structure-of-collagen-C-12-H-17-N-3-O-4.png)
Amino acid sequence constituting the primary structure of collagen C 12... | Download Scientific Diagram
![IJMS | Free Full-Text | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation IJMS | Free Full-Text | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation](https://www.mdpi.com/ijms/ijms-18-00549/article_deploy/html/images/ijms-18-00549-g001.png)
IJMS | Free Full-Text | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation
![After the peptide chain of collagen has been formed, many of the proline residues are hydroxylated on one of the ring carbon atoms. Why is this process important for the triple helix After the peptide chain of collagen has been formed, many of the proline residues are hydroxylated on one of the ring carbon atoms. Why is this process important for the triple helix](https://homework.study.com/cimages/multimages/16/screenshot_2022-07-02_150006450254088131518283.png)
After the peptide chain of collagen has been formed, many of the proline residues are hydroxylated on one of the ring carbon atoms. Why is this process important for the triple helix
![Cis/trans isomerization of proline peptide bonds in the backbone of cyclic disulfide‐bridged peptides - Sui - 2018 - Peptide Science - Wiley Online Library Cis/trans isomerization of proline peptide bonds in the backbone of cyclic disulfide‐bridged peptides - Sui - 2018 - Peptide Science - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/4c1a13d8-65e2-441a-a178-adf6fb9405f4/pep224088-toc-0001-m.png)
Cis/trans isomerization of proline peptide bonds in the backbone of cyclic disulfide‐bridged peptides - Sui - 2018 - Peptide Science - Wiley Online Library
![Aza-proline effectively mimics l -proline stereochemistry in triple helical collagen - Chemical Science (RSC Publishing) DOI:10.1039/C9SC02211B Aza-proline effectively mimics l -proline stereochemistry in triple helical collagen - Chemical Science (RSC Publishing) DOI:10.1039/C9SC02211B](https://pubs.rsc.org/image/article/2019/SC/c9sc02211b/c9sc02211b-f1_hi-res.gif)
Aza-proline effectively mimics l -proline stereochemistry in triple helical collagen - Chemical Science (RSC Publishing) DOI:10.1039/C9SC02211B
![Evidence of the Reduced Abundance of Proline cis Conformation in Protein Poly Proline Tracts | Journal of the American Chemical Society Evidence of the Reduced Abundance of Proline cis Conformation in Protein Poly Proline Tracts | Journal of the American Chemical Society](https://pubs.acs.org/cms/10.1021/jacs.0c02263/asset/images/large/ja0c02263_0005.jpeg)
Evidence of the Reduced Abundance of Proline cis Conformation in Protein Poly Proline Tracts | Journal of the American Chemical Society
![Proline N -oxides: modulators of the 3D conformation of linear peptides through “NO-turns” - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/C4OB00433G Proline N -oxides: modulators of the 3D conformation of linear peptides through “NO-turns” - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/C4OB00433G](https://pubs.rsc.org/image/article/2014/OB/c4ob00433g/c4ob00433g-f3_hi-res.gif)
Proline N -oxides: modulators of the 3D conformation of linear peptides through “NO-turns” - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/C4OB00433G
![Why are glycine and proline less commonly found in alpha helices than other amino acids? | Homework.Study.com Why are glycine and proline less commonly found in alpha helices than other amino acids? | Homework.Study.com](https://homework.study.com/cimages/multimages/16/1232502264899098957626.png)