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ap® biology 2008 scoring guidelines - AP Central
ap® biology 2008 scoring guidelines - AP Central

... This question tested knowledge of protein form and function from the basic to the applied level. Students were asked to describe the bonds involved with protein structure and apply their knowledge of protein structure to specific functions, such as muscle contraction, cell signaling, and enzyme regu ...
As listed in the Compendium of Pharmaceuticals and Specialties
As listed in the Compendium of Pharmaceuticals and Specialties

... The  systemic  availability  of  oral  glutathione  is  negligible;  the  vast  majority  of  it  must  be  manufactured  intracellularly  from  precursors.  Glutathione  is  a  tripeptide  made  intracellularly  from  its  constituent  amino  acids  L‐glutamate,  L‐cysteine  and  glycine.  The  sul ...
Deciphering the genetic code Dr. Syndey Brenner estabilished mRNA
Deciphering the genetic code Dr. Syndey Brenner estabilished mRNA

... complex binds to the small (40S) ribosomal subunit)  The cap at the 5’-end of the mRNA binds an initiation factor known as the cap-binding protein (CBP or eIF4F)---CBP contains a number of small subunits, including eIF4E  Several other eIFs join, and the mRNA then binds to the eIFs-MettRNAiMet-40S ...
protein sequence
protein sequence

Review Article
Review Article

... The eukaryotic cell has a wonderfully organized structure with many functionally specialized organelles, each bounded by one or more membranes that separate the organelle interior from other cellular compartments. Since the vast majority of polypeptides are synthesized in the cytosol, the cell is pr ...
Lecture3
Lecture3

... The word protein is a term from Greek word “PROTEIOS” meaning prime or primary. Proteins are essential organic constituent of living organism and are in the class of nutrient with highest concentration in muscle tissue of animals. ...
MCB_5255_files/feb 4 2015 MCB 5255 presentation
MCB_5255_files/feb 4 2015 MCB 5255 presentation

... the cytoplasm. Sometimes Hsp70 and Hsp90 function sequentially to fold the same protein  Cells are vigilant about getting these folds right because misfolded proteins can change the normal life of the cell. In some cases change is good, in others deadly. When HSP90 is compromised the number of mor ...
PowerPoint
PowerPoint

... First, we need a way to assign numbers to “shades of grey” matches. Genetic code scoring system – This assumes that changes in protein sequence arise from mutations. If only one point mutation is needed to change a given AA to another (at a specific position in alignment), the two amino-acids are mo ...
1 -2 -2 2 -3 I -1
1 -2 -2 2 -3 I -1

... Galton left his home and headed for a country fair… He believed that only a very few people had the characteristics necessary to keep societies healthy. He had devoted much of his career to measuring those characteristics, in fact, in order to prove that the vast majority of people did not have them ...
FTIR Analysis of Protein Structure
FTIR Analysis of Protein Structure

... are solved,2 some of these using the newer technique of multidimensional nuclear magnetic resonance spectroscopy (NMR). While X-ray crystallography and NMR spectroscopy provide the greatest level of detail about a protein’s structure, there are many situations where these techniques cannot be applie ...
2.3 Carbon-Based Molecules
2.3 Carbon-Based Molecules

... • Proteins are polymers of amino acid monomers. – Twenty different amino acids are used to build proteins in organisms. – Amino acids differ in side groups, or R groups. – Amino acids are linked by peptide bonds. ...
Chapter 3: Organic Molecules and life
Chapter 3: Organic Molecules and life

... * Is the sequence of amino acids important to a protein’s function? ...
Lecture 3 – Membrane potential
Lecture 3 – Membrane potential

... Lecture 3 – Different types of pumps An electrochemical gradient is a gradient of electrochemical potential, usually for an ion that can move across a membrane. The gradient consists of two parts, the chemical gradient, or difference in solute concentration across a membrane, and the electrical gra ...
Basics of Fluorescence
Basics of Fluorescence

... Tyrosine (abbreviated as Tyr or Y) is a nonessential amino acid with a polar side group. The word "tyrosine" is from the Greek tyros, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. ...
Honors Biology Name Cells Notes, continued… PROKARYOTIC
Honors Biology Name Cells Notes, continued… PROKARYOTIC

... 2. Membrane has pores surrounded by proteins which allow mRNA, tRNA, units of ribosomes and other large molecules to pass. 3. Contains DNA (normally in chromatin form) plus nucleolar regions. 4. Nucleolus: the nucleolar region is a densely clustered region of chromatin from several different chromos ...
Document
Document

... – These mutations may result in a new amino acid at a given position, the deletion of an amino acid, or the introduction of a new one. – Over VERY long periods of time two sequences may diverge so much that their relationship can not see seen through the direct comparison of their sequences. ...
SAM Teacher`s Guide Protein Partnering and Function - RI
SAM Teacher`s Guide Protein Partnering and Function - RI

... atoms and molecules. Atomic Structure is fundamental to understanding the structure  of atoms, including protons and electrons, which are essential for bonding.   Electrostatics focuses on the attraction of positive and negative charges. The  Intermolecular Attractions activity highlights the forces ...
Endoplasmic Reticulum Stress Response
Endoplasmic Reticulum Stress Response

... not be exposed in their native conformation. As a consequence, the ER contains a set of resident proteins called reticuplasmins, including enzymes and chaperones, that function in the synthesis, folding and assembly of newly synthesized proteins in the ER. 2.1.1 ER members of the HSP family: Binding ...
A Conserved Family of Nuclear Proteins Containing
A Conserved Family of Nuclear Proteins Containing

... Drosophila protein sequences deduced from the DNA sequences of serendipiry (Vincent et al., 1985) and of Kri@pel (Kr), a segmentation gene (Rosenberg et al., 1988). Aside from having in common the finger structure, these four and other finger proteins (see Berg, 1986) seem not to be directly related ...
Identification of genes and proteins involved in the
Identification of genes and proteins involved in the

... genes involved in arsenite oxidation and one in arsenite efflux as well as two proteins responsible for arsenate reduction were identified. Moreover, numerous genes and proteins belonging to various functional classes including information and regulation pathways, intermediary metabolism, cell envel ...
TG_ProteinPartners-ver10 - RI
TG_ProteinPartners-ver10 - RI

... atoms and molecules. Atomic Structure is fundamental to understanding the structure of atoms, including protons and electrons, which are essential for bonding. Electrostatics focuses on the attraction of positive and negative charges. The Intermolecular Attractions activity highlights the forces of ...
What makes cell membranes work? 9/23
What makes cell membranes work? 9/23

... What are the classes of protein one finds associated with the plasma membrane? Remember that not ALL membrane proteins may be free to diffuse about the membrane, some may be anchored to a particular place. ...
Spirulina - Sun Gates Center
Spirulina - Sun Gates Center

... A species of edible micro-algae, Spirulina is a complete protein known for its essential and non-essential amino acids…62% easily digested plant protein! Spirulina is blue - green algae high in chlorophyll, iron, carotenoids, anti-oxidants and other micronutrients. As is the case with all whole food ...
Chromatography - Union College
Chromatography - Union College

... The Ligand: Selection of the ligand for affinity chromatography is influenced by two factors: want specific and reversible binding affinity for the substance to be purified and chemically modifiable groups which allow it to be attached to the matrix without destroying its binding activity. Spacer Ar ...
Morphologically distinct phenotypes of spermatozoa in infertile men
Morphologically distinct phenotypes of spermatozoa in infertile men

... can be detected in human semen under electron microscopy: sperm with dysplasia of the fibrous sheath, non-specific flagellar defects, immotile cilia syndrome, acrosomal hypoplasia, defective chromatin condensation and compaction, pin head and sperm without heads. These conditions cannot be identifie ...
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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.
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