Design Layout References Mailingswords●●Endocrine System Part 2 Lecture-OBJECTIVES FOR PRE-LECTURE QUIZ #2●1. Recognize the following types of biomolecules when given images such as the ones belowand on the next page:● glucose (which is a monosaccharide)● triglycerides●ReviewphospholipidsDNA● RNAview•X English (United States)Add PenOFFDraw withTrackpadpolysaccharideamino acidprotein (recall a protein with less than 50 amino acids can also be called a peptidewhereas a protein with 50 or more amino acids can also called a polypeptide)steroidsDNAMacBook AirIFocusPage 2 of 10ER LayoutReferencesMarReview View+.Add PenTell meTrackpadMacBook AirXShare Com

Upper lane 1st image: Phospholipids 2nd image: amino acid 3rd image: glucose(which is a…

Answered: Recognize the following types of…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Please Aspa
Please answer all parts with explanations. This is biochemistry
The following figure is a diagram (cartoon or caricature) of the structure of a protein. What types of secondary structure are observed in the molecule? Is it a globular protein or a fibrous one?
The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false
Give typed explanation
What kind of interactions/bonds allow for the tight packing of saturated fatty acids? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a hydrogen bonds ionic bonds covalent bonds d van der Waals/ hydrophobic interactions e polar covalent bonds Unanswered 2 attempts left Submit
Consider this structure and choose the best descriptor below: This is an enzyme, and the active site is located at the far right. This is a DNA molecule, but not in the usual double-helix. This is a rather simple protein with no obvious.quaternary structure. This is a polysaccharide, with stacking sugars in the central region. None of these are apt for the given structure.
Consider this structure. CH3CH2 H CH2CH2CH C- H₂C 3 -C-CH₂ H Part 1 of 3 Give the IUPAC name of this structure. Part: 1/3 Part 2 of 3 Draw the skeletal structure. Part: 2/3 Part 3 of 3 Draw a constitutional isomer for this structure. Click and drag to start drawing a structure.
#13 Match the monomers (building blocks) to the biological polymers. (match each letter to the number it matches below) A.carbohydrates B.nucleic acids C.lipids D.proteins ----------------- 1.monosaccharides 2. glycerol and fatty acid chains 3. solutes and solvents 4. buffers 5. amino acids 6. nucleotides 7. water
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
Consider the 20 standard amino acids and their structures. Choose a set of 6 amino acids that you think could theoretically be eliminated from existence and still allow proteins to fold, function, and support life with the remaining 14. Eliminating amino acids from existence would result in a need for changes to the amino acid sequence of proteins, however your choices of amino acids to eliminate should result in minimal changes to the way proteins are currently structured and function. For each amino acid that you propose to eliminate defend your choice with a 2-3 point explanation using reasoning. Your answer should be no longer than 1.5 pages in length and you should start a new paragraph for each amino acid that you select to be eliminated.
Match the unique dehydration bonding that occurs with each specific macromolecule. [Choose ] this option is for nucleic acids peptide bond ester linkage glycosidic linkage Carbohydrates [ Choose ] Proteins [ Choose ] lipids [ Choose ] nucleic acids [ Choose ] > > >

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