![IJMS | Free Full-Text | Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima IJMS | Free Full-Text | Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima](https://www.mdpi.com/ijms/ijms-22-03029/article_deploy/html/images/ijms-22-03029-g001.png)
IJMS | Free Full-Text | Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima
3D Interaction Homology: Hydropathic Analyses of the “π–Cation” and “π–π” Interaction Motifs in Phenylalanine, Tyrosine, and Tryptophan Residues | Journal of Chemical Information and Modeling
![APH1 Polar Transmembrane Residues Regulate the Assembly and Activity of Presenilin Complexes - ScienceDirect APH1 Polar Transmembrane Residues Regulate the Assembly and Activity of Presenilin Complexes - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0021925818930589-gr1.jpg)
APH1 Polar Transmembrane Residues Regulate the Assembly and Activity of Presenilin Complexes - ScienceDirect
![Why are polar residues within the membrane core evolutionary conserved? - Illergård - 2011 - Proteins: Structure, Function, and Bioinformatics - Wiley Online Library Why are polar residues within the membrane core evolutionary conserved? - Illergård - 2011 - Proteins: Structure, Function, and Bioinformatics - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/a2889e3d-6f59-41a3-9ce4-d1ff126188d6/mfig001.jpg)
Why are polar residues within the membrane core evolutionary conserved? - Illergård - 2011 - Proteins: Structure, Function, and Bioinformatics - Wiley Online Library
![Partitioning of hydrophobic and polar residues between the surface and... | Download Scientific Diagram Partitioning of hydrophobic and polar residues between the surface and... | Download Scientific Diagram](https://www.researchgate.net/publication/12225905/figure/fig3/AS:267735678582809@1440844568576/Partitioning-of-hydrophobic-and-polar-residues-between-the-surface-and-interior-of-the.png)
Partitioning of hydrophobic and polar residues between the surface and... | Download Scientific Diagram
![Propensities of Polar and Aromatic Amino Acids in Noncanonical Interactions: Nonbonded Contacts Analysis of Protein−Ligand Complexes in Crystal Structures | Journal of Medicinal Chemistry Propensities of Polar and Aromatic Amino Acids in Noncanonical Interactions: Nonbonded Contacts Analysis of Protein−Ligand Complexes in Crystal Structures | Journal of Medicinal Chemistry](https://pubs.acs.org/cms/10.1021/jm061038a/asset/images/medium/jm061038an00001.gif)
Propensities of Polar and Aromatic Amino Acids in Noncanonical Interactions: Nonbonded Contacts Analysis of Protein−Ligand Complexes in Crystal Structures | Journal of Medicinal Chemistry
![Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations | PNAS Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations | PNAS](https://www.pnas.org/cms/10.1073/pnas.1221585110/asset/b38ad238-6b4f-4c4d-8869-ea1b92c98cc8/assets/graphic/pnas.1221585110fig03.jpeg)
Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations | PNAS
Conserved polar/charged residues (in red; numbering as in MOR) that... | Download Scientific Diagram
![How do non-polar residues (amino acid side chains) interact with other residues? How do polar residues interact with other residues? With water? How do charged residues interact with other residues? | Homework.Study.com How do non-polar residues (amino acid side chains) interact with other residues? How do polar residues interact with other residues? With water? How do charged residues interact with other residues? | Homework.Study.com](https://homework.study.com/cimages/videopreview/videopreview-full/pg61s4gvmq.jpg)
How do non-polar residues (amino acid side chains) interact with other residues? How do polar residues interact with other residues? With water? How do charged residues interact with other residues? | Homework.Study.com
![SOLVED: It depends on the occurrence of polar and nonpolar residues in sequence: Peptide #1 has every residue so it has more chance to be helical. On the other hand; peptide #2 SOLVED: It depends on the occurrence of polar and nonpolar residues in sequence: Peptide #1 has every residue so it has more chance to be helical. On the other hand; peptide #2](https://cdn.numerade.com/ask_images/bdea8c24b0b245db942ca6f35134c053.jpg)
SOLVED: It depends on the occurrence of polar and nonpolar residues in sequence: Peptide #1 has every residue so it has more chance to be helical. On the other hand; peptide #2
![Polar and apolar residues are segregated in AMPs to form amphilphilic... | Download Scientific Diagram Polar and apolar residues are segregated in AMPs to form amphilphilic... | Download Scientific Diagram](https://www.researchgate.net/publication/259158305/figure/fig4/AS:702633895538691@1544532383446/Polar-and-apolar-residues-are-segregated-in-AMPs-to-form-amphilphilic-structures-A-The.png)
Polar and apolar residues are segregated in AMPs to form amphilphilic... | Download Scientific Diagram
![PDF] On the significance of alternating patterns of polar and non-polar residues in beta-strands. | Semantic Scholar PDF] On the significance of alternating patterns of polar and non-polar residues in beta-strands. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/adc75e0f5e2d2d3c7ff74b6baa12a8882f1ff860/6-Table2-1.png)
PDF] On the significance of alternating patterns of polar and non-polar residues in beta-strands. | Semantic Scholar
![Exposure to the solvent of polar, non-polar and charged residues along the folding trajectories pertaining to three different knotting mechanisms, plotted as a function of the RMSD to the native structure. Exposure to the solvent of polar, non-polar and charged residues along the folding trajectories pertaining to three different knotting mechanisms, plotted as a function of the RMSD to the native structure.](https://s3-eu-west-1.amazonaws.com/ppreviews-plos-725668748/995013/preview.jpg)