• 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
Most common elements in living things are carbon, hydrogen
Most common elements in living things are carbon, hydrogen

... Elements & Macromolecules in Organisms Most common elements in living things are carbon, hydrogen, nitrogen, and oxygen. These four elements constitute about 95% of your body weight. All compounds can be classified in two broad categories --- organic and inorganic compounds. Organic compounds are ma ...
Chapter 6 Proteins and Amino Acids I Introduction II The Structure of
Chapter 6 Proteins and Amino Acids I Introduction II The Structure of

... C. Carla has been following a high proteina and low carbohydrate diet. Explain what would happen to much of the protein she is eating. D. Don has been eating a diet with plenty of foods containing carbohydrate and protein. What happens to the protein in his foods? E. Which can the body use to make g ...
3 MoleculesCells
3 MoleculesCells

... monomers are they made of? What types of glycosidic bonds do they have? What is the structural differences between the storage polysaccharides? Where are each found in nature? 4. Which polysaccharides are used for structural support in living things? How are they constructed with regards to monosacc ...
slides
slides

... 1. For homologous proteins (similar ancestry), this provides the “gold standard” for sequence alignment--elucidates the common ancestry of the proteins. 2. For nonhomologous proteins, allows us to identify common substructures of interest. 3. Allows us to classify proteins into clusters, based on st ...
EB Protein Structure - New Paltz Central School District
EB Protein Structure - New Paltz Central School District

... linking NH2 of 1 amino acid to COOH of another  C–N bond ...
A Story About Cakes
A Story About Cakes

... 3. To make sure the recipe isn’t lost or tampered with, he photocopies it to go to the kitchen ...
Proteins
Proteins

... linking NH2 of 1 amino acid to COOH of another  C–N bond ...
pH - Bio-Link
pH - Bio-Link

... dehydrate an organism’s body more than half of the cellular dry weight would be protein. It is estimated that the typical mammalian cell has at least 10,000 different proteins. Proteins are the macromolecules of the cell that “make things happen.” Proteins determine much of what moves in and out of ...
Exam1
Exam1

... B) do not have as many disulfide crosslinks between adjacent strands. C) do not stack in sheets as well as antiparallel strands. D) have fewer lateral hydrogen bonds than antiparallel strands. E) have weaker hydrogen bonds laterally between adjacent strands. ...
a  version - SEA
a version - SEA

... proteins in bacteriophage genomes. Proteins from Superfamilies IV and VII, and Family 1.E.18 have been found in phages that infect the hosts Mycobacterium and Gordonia. There are indications that proteins from Superfamilies I, II and III may be present, but we have found no evidence for holins from ...
Structure of a protein - Campus
Structure of a protein - Campus

... Functions of proteins in organisms Proteins perform functions of growth and of support, but also more sophisticated roles, linked for example to defence, regulation and catalysis. The main functions ...
protein review
protein review

... - regular coiling and folding of pp regions - resultant repeated patterns is 2o structure - by regularly spaced H-bonds formed at the pp backbone between NH group of one Aa & C=O group of other Aa - H-bonds DO NOT involve R groups. - α-helix and β-pleated sheet. ...
Protein
Protein

... living things. They can store twice as many calories as polysaccharides can. Oils (mostly from plants) contain more unsaturated fatty acids, while fats (animals) contain more saturated fatty acids.  Simple lipids also dissolve vitamins ...
Topic 4: BIOLOGICALLY IMPORTANT ORGANIC MOLECULES
Topic 4: BIOLOGICALLY IMPORTANT ORGANIC MOLECULES

... (2) there are many H-C bonds which means that the molecule has a very high energy storage content; these are often referred to as “depot” lipids. (3) the hydrogen tails may have singly C-C (“saturated”) and doubly C=C (“unsaturated’) bonded carbons. Presence of a double bond introduces a bend in the ...
Function of plasma protein in diagnosis of animal disease
Function of plasma protein in diagnosis of animal disease

... of diseases and conditions. • It can be used for these purposes because the levels of different blood proteins rise or fall in response to such disorders as cancer, intestinal or kidney protein-wasting syndromes, disorders of the immune system, liver dysfunction, impaired nutrition, and ...
Biology: Exploring Life Resource Pro
Biology: Exploring Life Resource Pro

... molecules. Hydrocarbons are organic molecules composed of only carbon and hydrogen. Different arrangements of atoms bonded to a carbon skeleton can form functional groups, which give specific properties to molecules. For example, hydroxyl groups (–OH) are hydrophilic, meaning they attract water. Mol ...
7.3 Structures and Organelles
7.3 Structures and Organelles

... · surrounded by a membrane and contain membrane-bound organelles that perform specific functions · the organelles are anchored in the cytoplasm by the cytoskeleton - a network of protein fibers · ROLE: structural support and to help move organelles ...
Topic 4 - FSU Biology
Topic 4 - FSU Biology

... polypeptides (proteins) -very large polymers of amino acids (>20) Proteins are an extremely diverse group of macromolecules; a given cell may express 104 different kinds of proteins- function in structure, support, catalysis, chemical communication (hormones, neurotransmitters) , membrane transport. ...
長榮管理學院九十學年度二年制技術學系招生考試
長榮管理學院九十學年度二年制技術學系招生考試

... 9. Which of the following most accurately describes the charge state of DNA under physiological conditions? a. Roughly uniformly positively charged along its length b. Roughly uniformly negatively charged along its length c. Roughly uniformly uncharged along its length d. Heterogeneously charged, wi ...
4/3
4/3

... Difficulties in designing protein chips • Unique process is necessary for constructing each probe element • Challenging to produce and purify each protein on chip • Proteins can be hydrophobic or hydrophilic – Difficult to design a chip that can detect both ...
Chapter 3: Section 3.2
Chapter 3: Section 3.2

... are bonded together by peptide bonds – made from combinations of 20 amino acids – Used in structural material, enzymes, cell transport, cell structure, & antibodies – Examples: keratin (hair & skin), albumin (egg whites), Hemoglobin (carries O2 in blood), Myosin (muscle) ...
Lecture 12: Enzyme Catalysis Topics: Catalytic Strategies Steps in a
Lecture 12: Enzyme Catalysis Topics: Catalytic Strategies Steps in a

... The affinity of hemoglobin for oxygen can be regulated by allosteric effectors to improve its physiological performance. Key Concepts: Function of hemoglobin Conformational changes due to oxygen binding Cooperativity Role of BPG ...
PROTEIN[1]
PROTEIN[1]

... as calcium, zinc, and Vitamin B6 • Transferrin transports iron (hemoglobin – a protein, contains iron, but it transports oxygen) • Proteins may also acts as channels or pumps across the cell membrane ...
2.3 Study Guide - Issaquah Connect
2.3 Study Guide - Issaquah Connect

... broken down as a source of chemical energy; part of cell structure functions including movement, transport, chemical catalysts ...
RNA and Protein Synthesis
RNA and Protein Synthesis

... 20. Describe the structure of proteins. A series of amino acids bonded together with peptide bonds. Enzymes 21. What organic compound are enzymes composed of?__proteins__How are they typically named (think word parts)? They typically end in “ase” 22. What happens to enzymes during/after a chemical r ...
< 1 ... 531 532 533 534 535 536 537 538 539 ... 656 >

Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
  • studyres.com © 2025
  • DMCA
  • Privacy
  • Terms
  • Report