Protein Structure, Folding and Function notes
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This GoConqr page gathers university-level notes on Protein Structure, Folding and Function, from amino acids to collagen and protein function. University students and professional candidates can use them to revise these topics, while teachers can find material for teaching. There are more than 10 notes to explore. Pick a note to begin.
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- Amino acid structure and properties79
- Peptides and peptide bonds18
- Levels of protein structure30
- Protein domains and structural interactions9
- Protein folding and denaturation19
- Molecular chaperones8
- Protein misfolding and disease7
- Protein-ligand binding11
- Hemoglobin and myoglobin39
- Globular and fibrous proteins11
- Protein analysis and sequencing14
Notes
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Four Levels of Protein Structure Primary structure describes the linear sequence of amino acid residues in a protein. The sequence of amino acids determines the structural and functional characteristics of the protein. Proteins with very different se...
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Protein III: collagen Collagen is an insoluble fibrous protein and is the most common protein in mammals. 33% of bone and 50% of cartilage is made of collagen it also surrounds cells. As it is insoluble a soluble precursor tropocollagen is...
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Proteins: terminology and alpha helix Definitions PROTEIN: molecular mass greater than 5000 daltons made up of L-amino acids s linked together end to end by peptide bonds. Smaller molecules are called polypeptides. SIMPLE PROTEINS yield only amino acids w...
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Structure and function of Proteins - created from Mind Map
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Myoglobin and Haemoglobin HaemThe haem(UK)/heme(USA) prosthetic group is necessary for myoglobin and haemoglobin to bind to oxygen. The difference between protoporphyrin XI and haem is a central Fe molecule. Structure of myoglobinIt polypeptid...
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Untitled ANSWER: - POINT ONE (WHAT ARE THE TYPES OF NON-COVALENT INTERACTIONS PRESENT IN PROTEIN MOLECULES?) Non-covalent interactions are the types of bonds that are not as strong as covalent bonds although ...
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Protein Lessons Amino acids and the primary structure 20 kinds of amino acids used in protein synthesis Amino acids are also precursors to other useful molecules Always the L-stereoisomer (except Glycine) Classed according to ...
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Location of hydrophobic and hydrophilic amino acids in proteins Hydrophilic molecules or ions are surrounded by water molecules with which they interact by electrostatic or hydrogen bondsHydrophobic molecules are unable to interact with water, they tend to be insoluble and instead...
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Protein Analysis - neurological disorders Neurological disorders often have a spectrum: - suggesting different genetic basis and multiple genes - many proteins can be implicated in a single disorder - display variations in clinical severity and pr...
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Protein function Enzymes catalyze the biochemical reactions that occur in cells by lowering the activation energy necessary to transform a reactant into a product. Kinases add phosphate groups to proteins (phosphorylate...
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Untitled Primary structure is simply the sequence of amino acids in a polypeptide chain. For example, the hormone insulin has two polypeptide chains. Each chain has its own set of amino acids, assembled in a particul...
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Notes for 9/24/2014 Chapter 5 - Function of ProteinsFunction of Globular Proteins Cellular structure Transport Storage Recognition and/or defense Muscle Contraction Catalysis Ligand Binding Ligand - a molecule or ion th...
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Untitled Peptides and Proteins • polymers of amino acids • biologically occurring polypeptides range in size from small to very large, consisting of two or three to thousands of linked amino acid residues • two amino acid mole...
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Proteins Amir Khan Peptide Bond: Proteins are linear sequences of amino acids which are linked together by a peptide bond. Peptide bond formed by the alpha amino acid group and the alpha carboxyl group of another Once the amino acids jo...
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CC 1A Notes FC1-1A Amino Acids DESCRIPTION Absolute configuration at the α position Amino acids as dipolar ions Classifications Acidic or basic Amino acids w/ acidic side groups carry a net negative charge a physiologic pH Hydrop...
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Alpha Helices Because Hydrogen bonding is not available to stabilize amino acids on either end of the helix, the amino terminus is partially negative
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Amino Acids BASIC STRUCTURE different types: 1. non-polar amino acids 2.
More Protein Structure, Folding and Function resources
About protein structure, folding and function notes
GoConqr OriginalProtein structure, folding and function notes
These user-made notes offer different routes through the unit. Proteins: terminology and alpha helix introduces protein terminology, while Four Levels of Protein Structure begins with the sequence of amino acids. For a starting point, choose the latter if you want to review how a protein is organised.
Other notes focus on particular proteins or roles. Protein III: collagen discusses collagen, and Myoglobin and Haemoglobin looks at proteins that bind oxygen. Protein function includes enzymes and their roles in reactions.
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Frequently asked questions
Which note is a good place to start?
Four Levels of Protein Structure is a useful starting point if you want to review how proteins are organised. It begins with the sequence of amino acids. For terminology and alpha helices, you could instead start with Proteins: terminology and alpha helix.
What topics do the notes cover?
The notes include amino acids, protein terminology, alpha helices and the levels of protein structure. They also cover particular proteins, including collagen, myoglobin and haemoglobin, as well as protein functions such as enzyme activity. Each note offers a different focus within the unit.
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Yes. Every note listed here is free to open and study without an account. The resources were made by GoConqr users. A free account also lets you save quiz scores and make your own quizzes, mind maps, flashcards and notes.