The amino acids Gly and Pro, as well as modified prolines that have a hydroxy group on the Pro ring or Hyp, are the principal amino acids comprising collagen. Consider this excerpt from this article: Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycineKonrad Beck, Virginia C. Chan, Nigel Shenoy, Alan Kirkpatrick, John A. M. Ramshaw, and Barbara BrodskyPNAS April 11, 2000 97 (8) 4273-4278; https://doi.org/10.1073/pnas.070050097 “Gly-Pro-Hyp is the most common, as well as the most stabilizing, triplet in collagen (5). The presence of Gly at every third residue is considered essential….” If there is a genetic mutation that interrupts this pattern of Gly at every third position, bones do not develop properly. They are characteristically brittle, resulting in a genetic disease known as osteogenesis imperfecta. Use your knowledge of the structure of collagen to explain why this regularly repeating Gly residue is essential to the formation of a proper and strong collagen triple helix?  (2 pts.) Vitamin C is required for the biochemical reaction that puts the modifying OH group on a Pro in collagen. Why does a vitamin C deficiency result in changing the overall strength of collagen? (2 pts.)

In the Jewish faith, a memorial service; literally meaning, “God full of compassion”, usually the last prayer of the funeral service

For 30 days after someone of the Jewish faith dies, mourners must abstain from amusement and festivities and even refrain from work; This is called__________________________

Questions 2–9 refer to this toxic peptide. General Instructions: If the question does not require you to draw a structure, you may answer using either the full name of an amino acid or use its three-letter or single-letter code.   Many animal toxins are peptides. One of these is a 42-residue toxic peptide found in the South American rattlesnake, Crotalus durissus terrifics. The primary sequence of this peptide is shown below and its structure is shown in the figure. YKQCHKKGGHCFPKEKICLPPSSDFGKMDCRWRWKCCKKGSG Image Description  A 3D protein structure showing the positions of cysteine residues (Cys4, Cys11, Cys18, Cys30, Cys36, and Cys37) highlighted in yellow. The protein has an N-terminal (N) and C-terminal (C) with distinct secondary structures: alpha-helices in red and beta-sheets in blue, connected by green loops. The cysteine residues form disulfide bonds, contributing to the protein’s stability and shape.

A symbolic cloth covering placed over a casket

What is the casket used in a Jewish Orthodox funeral called?

This is the reference to an article that appeared recently in the journal Nature about a protein secreted by pathogenic bacteria that cause brown spot in beans, bacterial spec in tomatoes and fire blight in fruit trees. These bacteria infect plant cells, causing them to “drain” cell material leading to cell death. Because of the economic impact of this infection, groups have worked for years to elucidate the mechanism by which this protein infects plant cells. The Nature article reports that alpha fold in combination with cryo EM produced a protein structure that led to the solution of this 30 year old puzzle.  Below is a portion of the text from the article along with one of the figure depicting the structure of the protein.  Based upon the structural information in the text and the figure, suggest a possible way this protein could “drain” a plant cell such that, cell death results. Image Description  AlphaFold2 analysis and cryo-EM imagingTo gain functional insights into the AvrE family of bacterial effectors, we constructed their three-dimensional models predicted by AlphaFold226 using the fast homology search of MMseqs2 (ColabFold) 27. The predicted AlphaFold2 models of DspE from E. amylovora, DspE from P. carotovorum, AvrE from P. syringae pv. tomato (Pst) DC3000 and WtsE from P. stewartii (Fig. 1 and Extended Data Figs. 1 and 2) all reveal an overall similar architecture resembling a mushroom, with a prominent central ẞ-barrel forming the stem, which is surrounded by a globular amino-terminal domain (E. amylovora DspE: K298-H672), a WD40 repeat domain (H673-P912) and two perpendicularly arranged helix bundles (E998-T1222 and A1567-H1647) on the top. The predicted domain arrangement is supported by our cryo- EM imaging of E. amylovora DspE, for which the two-dimensional class averages clearly reveal an overall similar top view to that of the AlphaFold model, with circularly arranged globular domains surrounding a central pore (Fig. 1a,b). Image Description  Fig. 1: Model and cryo-EM images of E. amylovora DspE. (a) Three-dimensional model generated by AlphaFold2 using MMseqs2 (ColabFold). DspE (residues 298–1838) is shown in a rainbow color gradient, with the N terminus in blue and the C terminus in red. (b) Cryo-EM two-dimensional class averages of DspE, revealing a circular arrangement of domains around a pore. Scale bars, 5 nm. (c) Surface representation of DspE. (d) Sliced view of DspE. In (c, d), residues are colored based on hydrophobicity. of their hydrophobicity.            

In a Type 4 device, what is the minimum number of recording parameters?

Sephadex G-75 is a gel filtration or size exclusion solid phase chromatography material. It has it has a molecular weight cutoff range of >80 kD, where kD stands for kiloDalton (1 Dalton is 1 atomic mass unit). Briefly describe how this column functions and is able to separate a protein with a molecular weight of 100 kD from a protein with a molecular weight of 45 kD.

Hemoglobin (Hb) consists of 4 separate polypeptide chains, two