• Study Resource
  • Explore Categories
    • Arts & Humanities
    • Business
    • Engineering & Technology
    • Foreign Language
    • History
    • Math
    • Science
    • Social Science

    Top subcategories

    • Advanced Math
    • Algebra
    • Basic Math
    • Calculus
    • Geometry
    • Linear Algebra
    • Pre-Algebra
    • Pre-Calculus
    • Statistics And Probability
    • Trigonometry
    • other →

    Top subcategories

    • Astronomy
    • Astrophysics
    • Biology
    • Chemistry
    • Earth Science
    • Environmental Science
    • Health Science
    • Physics
    • other →

    Top subcategories

    • Anthropology
    • Law
    • Political Science
    • Psychology
    • Sociology
    • other →

    Top subcategories

    • Accounting
    • Economics
    • Finance
    • Management
    • other →

    Top subcategories

    • Aerospace Engineering
    • Bioengineering
    • Chemical Engineering
    • Civil Engineering
    • Computer Science
    • Electrical Engineering
    • Industrial Engineering
    • Mechanical Engineering
    • Web Design
    • other →

    Top subcategories

    • Architecture
    • Communications
    • English
    • Gender Studies
    • Music
    • Performing Arts
    • Philosophy
    • Religious Studies
    • Writing
    • other →

    Top subcategories

    • Ancient History
    • European History
    • US History
    • World History
    • other →

    Top subcategories

    • Croatian
    • Czech
    • Finnish
    • Greek
    • Hindi
    • Japanese
    • Korean
    • Persian
    • Swedish
    • Turkish
    • other →
 
Profile Documents Logout
Upload
Amino acids
Amino acids

... and van der Waals interactions among hydrophobic R groups. – While these three interactions are relatively weak, strong covalent bonds called disulfide bridges that form between the sulfhydryl groups (SH) of two cysteine monomers act to rivet parts of the protein together. ...
Protein glycosylation in pathogenic and non
Protein glycosylation in pathogenic and non

... What kind of questions can we ask using microorganisms?  Model systems!  "From the elephant to butyric acid bacterium—it is all ...
2. Structure and bonding of carbohydrates, proteins and lipids
2. Structure and bonding of carbohydrates, proteins and lipids

... inside the membrane with that outside the membrane. Semi-permeable membranes allow for the possibility of a different intracellular milieu from the environment. This makes the single cell into an organism. In multi-cell organisms, membranes make differentiated functioning possible. Cells can have di ...
biochem ch 7 [12-11
biochem ch 7 [12-11

... o Charged polar AA side chains generally located on surface of protein, where they form ion pairs (salt bridges, ionic interactions) or are in contact with aqueous solvent; charged side chains often bind inorganic ions to decrease repulsion between like charges  When charged amino acids located on ...
Secretory Protein mRNA Finds Another Way Out
Secretory Protein mRNA Finds Another Way Out

... within the same cell, others are secreted. One property that differentiates secretory proteins from cell-bound proteins is their signal sequence, which recruits protein complexes that grab the new protein while it’s still being translated and targets it to the endoplasmic reticulum (ER), where it wi ...
Area 4: Molecular recognition in biomolecules Computational
Area 4: Molecular recognition in biomolecules Computational

... Tel. +39.06.49917916 e-mail: [email protected] ...
Identification of RIG-I CARD Interacting Cellular Proteins Poh
Identification of RIG-I CARD Interacting Cellular Proteins Poh

... endogenous interacting proteins with RIG-I CARD as the levels of expression might be too low. Thus it is impossible to make a concrete deduction from the observed interaction of Hsp70 with CARD. Also, most protein bands (P2-P10) are shown to be cleavage products of the expressed constructs, possibly ...
Nutritional biochemistry
Nutritional biochemistry

... 4. Acidic a. a. and negative charge-R side chain: e.g. aspartic acid-glutamic acid. Structure of aspartic acid (Asp): ...
Insilico drug design
Insilico drug design

... • Uses the 3D structure of the target receptor to search for the potential candidate compounds that can modulate the target function. • These involve molecular docking of each compound in the chemical database into the binding site of the target and predicting the electrostatic fit between them. • T ...
Name- Kristin Kaufmann
Name- Kristin Kaufmann

... 1) Compare the hydrophobic forces that hold a membrane protein in the lipid bilayer to those that help proteins fold into unique three-dimensional structures. The hydrophobic forces that hold a protein in the lipid bilayer into the membrane are interactions between the fatty acid tails and the amino ...
Kidney Disease and Protein
Kidney Disease and Protein

... Your dietitian can help you decide if any of these types of products would help and which ones are better than others for you. How can I increase the amount of protein I eat? Here are some tips to increase the amount of protein in your diet every day:  Eat your biggest meal at a time in the day whe ...
Macs Notes
Macs Notes

... that BREAK DOWN molecules.)  Water is used during the process. Why? b/c now you have to break up one or more of the covalent links. This leaves unhappy atoms with electrons that need to be shared. So...  ...water breaks up into –H and –OH and attaches to make each side happy.  In the body these r ...
Bma: Visual Tool for Modeling and Analyzing Biological
Bma: Visual Tool for Modeling and Analyzing Biological

... Motivated by sbml [10], bma supports output to a custom xml format. Thus, it is possible to interface other analysis tools with bma models. ...
Biol115_2014_Lecture 8_Protein Structure
Biol115_2014_Lecture 8_Protein Structure

... • Associate protein structure to function. • Key terms: alpha helix, amino acid, beta pleated sheet, catalyst, denaturation, disulphide bridge, hydrophobic effect, peptide bond, polypeptide, primary structure, protein, quaternary structure, secondary structure, tertiary structure, Xray crystallograp ...
4 slides pdf
4 slides pdf

... interactions between side chains in different regions. – results in domains, basic units of tertiary structure Quaternary structure: interactions between different polypeptide chains in proteins composed of more than one polypeptide ...
ppt
ppt

... BL 424 Ch. 2 Review Composition of Cells Cell biology seeks to understand cellular processes in terms of chemical, physical reactions Student Learning Outcomes: A. To describe molecular composition of cells: Carbohydrates, lipids, nucleic acids, proteins  Draw phospholipid structures, sugars, amino ...
Survival of the Fittest Molecule
Survival of the Fittest Molecule

... genes that cause specific protein changes, including hemophilia, muscular dystrophy and sickle cell anemia. While some of these altered-protein diseases remain difficult to correct, others can be treated. In the case of classic hemophilia, replacing the bloodclotting factor VIII protein that is miss ...
Primary Structure Specifies Tertiary Structure
Primary Structure Specifies Tertiary Structure

PPT - AePIC
PPT - AePIC

... Conformational changes Protein folding Molecular recognition (drug design) Ion transport The method is based on the Newton’s equation of motion: ...
protein intake for optimal muscle maintenance
protein intake for optimal muscle maintenance

... make on its own and thus, these amino acids must come from the foods we eat. A complete protein is named just that because it will contain all of the essential amino acids our body needs to repair and grow. These proteins sources are animal-based and include meat, poultry, fish, eggs and cheese. Foo ...
02-3 Carbon Compounds
02-3 Carbon Compounds

... • Lipids are involved mainly with long-term energy storage. They are generally insoluble in polar substances such as water. • Mostly contain C and H atoms. • Secondary functions of lipids are as structural components (the major building block in cell membranes) and as "messengers" (hormones) that pl ...
Bacteriology lecture no 5 2nd class *The Neisseriae
Bacteriology lecture no 5 2nd class *The Neisseriae

... B-Por.por protein extend through the gonococcal cell membrane ,it occur in trimers to form pores in the surface through which some nutrient enter the cells .Por protein may impact intracellular killing of gonococci within neutrophil by preventing phagosome lysozyme fusion. C-Opa protein :These prote ...
The stuff of life?
The stuff of life?

... Proteins - modified carbon skeleton backbone: backbone is amino + carbon + carboxylic acid, plus many diverse functional groups monomers: amino acids polymers: peptides/proteins enzymes Microtubules Hemoglobin Membrane proteins ...
Mass spectrometry and proteomics Steven P Gygi* and Ruedi
Mass spectrometry and proteomics Steven P Gygi* and Ruedi

... that is covalently derivatized with trypsin. The generated peptides are then trapped on a membrane and identified by MALDI−TOF mass fingerprinting. The overall 2DE−MS approach has been used to generate annotated 2D gel databases for a myriad of cell types from different species. A partial list of su ...
poster (ppt file) - The Leitzel Center
poster (ppt file) - The Leitzel Center

... If the receptor site is exposed to either gas the enzyme will become inert and unable to catalyze H2. [3] There are two types of hydrogenase classified by metals at their activation site. Both [FeNi]-hydrogenase (Figure 1) and [FeFe]-hydrogenase are naturally occurring and are studied for their pote ...
< 1 ... 351 352 353 354 355 356 357 358 359 ... 520 >

Protein–protein interaction



Protein–protein interactions (PPIs) refer to physical contacts established between two or more proteins as a result of biochemical events and/or electrostatic forces.In fact, proteins are vital macromolecules, at both cellular and systemic levels, but they rarely act alone. Diverse essential molecular processes within a cell are carried out by molecular machines that are built from a large number of protein components organized by their PPIs. Indeed, these interactions are at the core of the entire interactomics system of any living cell and so, unsurprisingly, aberrant PPIs are on the basis of multiple diseases, such as Creutzfeld-Jacob, Alzheimer's disease, and cancer.PPIs have been studied from different perspectives: biochemistry, quantum chemistry, molecular dynamics, signal transduction, among others. All this information enables the creation of large protein interaction networks – similar to metabolic or genetic/epigenetic networks – that empower the current knowledge on biochemical cascades and disease pathogenesis, as well as provide putative new therapeutic targets.
  • studyres.com © 2026
  • DMCA
  • Privacy
  • Terms
  • Report