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Supplemental Methods 1. Amino acid conformation clustering Amino
Supplemental Methods 1. Amino acid conformation clustering Amino

... Atomistic contact interactions in proteins of known structures were organized into a database containing non-covalent atomistic interaction information for atom pairs in protein structures. The general methodology is outline in Figure S1. For each of the atoms in residue X of a protein, the non-cova ...
Fats - Cobb Learning
Fats - Cobb Learning

... Dietary fiber is not digestible in humans and thus provides no calories. ...
Etoposide Phosphate Enhances the Acetylation Level
Etoposide Phosphate Enhances the Acetylation Level

... Protein synthesis in eukaryotic cells is a complicated process which requires hundreds of proteins and RNAs. The translation process includes three phases: initiation, elongation, and termination. Many studies indicated that the regulation of the elongation phase can be important during the cell cyc ...
C. Sulfonamides
C. Sulfonamides

...  The sulfonamide and the amino group must be directly attached to the ring and in P position to each other.  Any extra substitution will reduce activity.  Sulfonamide nitrogen must be either primary or secondary. ...
Solid Tumour Section Ovary: inv(10)(q11q11) in ovarian germ cell tumors
Solid Tumour Section Ovary: inv(10)(q11q11) in ovarian germ cell tumors

... Diagrammatic representation of RET/NCOA4 (PTC3) fusion protein. Amino acids surrounding each breakpoint (arrows) are indicated, and numbered according to their position within RET or NCOA4, respectively. Peptide sequences from RET are in red, from NCOA4 in green. The transmembrane domain (TM) of RET ...
SeeProtStructFromPDB
SeeProtStructFromPDB

... As you can see from this structure, in the mutation that causes hemochromatosis, a cysteine residue that is involved in a disulfide bridge is mutated. The disulfide bond holds together two regions of the hemochromatosis protein. When the cysteine residue is replaced by another amino acid, tyrosine, ...
5 Lipid and Protein Metabolism
5 Lipid and Protein Metabolism

... fatty acid metabolism during fasting or carbohydrate restriction to use as energy instead of glucose • 2 of the 3 are used by the heart and brain and muscle for ATP synthesis – Picked up by cells and used to make acetyl-CoA – In the brain ...
CHAPTER 1 PATHOGENESIS OF GOUSIEKTE  1.1
CHAPTER 1 PATHOGENESIS OF GOUSIEKTE 1.1

... Titin in the I-band exhibits elastic behaviour upon sarcomeric stretch, contributing to the passive tension of cardiac muscle (Fig. 2.1). The extensible I-band region of titin has multiple segments: the tandemly arranged Ig (immunoglobulin-like) segments, N2B, N2A and the PEVK region, so called beca ...
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invited talk

... The RFN elements ...
Document
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... A rich array of puromycin analogues with modified amino acid, carbohydrate, and/or base moieties has been prepared and evaluated biologically to study the structure-activity correlations….. ...
Chapter 2b Packet answers
Chapter 2b Packet answers

... Chapter 2b Extra Practice1. All organic compounds contain _carbon____________. 2. Without _energy___, organisms could NOT maintain homeostasis, carry out chemical reactions, make their own food. 3. The ability to move or change matter is __energy____________________. 4. All living things require a ...
2009_outline_5
2009_outline_5

The Invention of Proteomic Code and mRNA
The Invention of Proteomic Code and mRNA

... as the chief proponent of the Big Bang theory in cosmology. He proposed a Diamond Code [4-6] where DNA acted directly as a template for assembling amino acids into proteins. Various combinations of bases along one of the grooves in the double helix could form distinctively shaped cavities into which ...
Genetically engineered gold-binding polypeptides
Genetically engineered gold-binding polypeptides

... interest to biologists and biotechnologists studying hard tissue growth and regeneration, as well as to materials scientists using biomimetic approaches for the control of inorganic material fabrication and assembly. Biomimetics requires an accurate understanding of natural mechanisms at the molecul ...
Quiz 2 Review Sheet
Quiz 2 Review Sheet

... each level… Know all the details we went over in class like when the side chains come into play or when only the backbone is involved, hydrophobic vs hydrophilic side chains, where different types of side chains are located in proteins typically, etc… 50.5. All alpha helices are right or left handed ...
Boronophenyl analogs of phospholyrosines
Boronophenyl analogs of phospholyrosines

... speci?c contacts for assembly of receptor signaling com plexes has provided a breakthrough in understanding signal ...
Protein Structure Analysis - G
Protein Structure Analysis - G

Infrared spectroscopy: a tool for protein characterization Chenge Li
Infrared spectroscopy: a tool for protein characterization Chenge Li

... Proteins are relatively large, compact, structurally complex molecules that are made from small molecules called amino acids. Amino acids share a common structure, which contains an amino group (-NH2), a carboxyl group (-COOH), along with a side chain that is specific for each amino acid. The side c ...
View as PDF document
View as PDF document

... acetylcholinesterase gene and the protein it encodes can be used to demonstrate a number of biological concepts, including enzyme specificity, competitive inhibition, mutation, characteristics of the genetic code, alternate splice sites, natural selection, bioinformatics, and disease transmission. M ...
Coupling Coherence Distinguishes Structure Sensitivity in Protein
Coupling Coherence Distinguishes Structure Sensitivity in Protein

... rates occurs in the small C multiple-pathway regime. Because small C values have been computed in nonheme proteins as well, we can further explore the correlation between small C values and exponential distance decay. Previous theoretical analysis of the blue-copper protein azurin indicates that all ...
An amino acid contains an amino group, a carboxyl
An amino acid contains an amino group, a carboxyl

Hamster Placental Lactogen-ll Contains a Structural Feature Unique
Hamster Placental Lactogen-ll Contains a Structural Feature Unique

... bond with a serum protein, generating the high Mr disulfide-bonded form of haPL-ll. It is not possible at this time to predict which of the Cys residues of haPLII participate in the formation of an intermolecular disulfide bond. It has become increasingly clear that the placenta is the source of a n ...
Cloning and expression of maize-leaf pyruvate, Pi dikinase
Cloning and expression of maize-leaf pyruvate, Pi dikinase

... We then proceeded to clone the corresponding cDNA for the ZmGI TC220929 gene (GenBank Accession No. AY106855) by screening a maize leaf cDNA library with a cloned 491 bp PCR fragment complementary to sequences internal to the respective AY106855 ORF. Screening of the library with this 491 bp 32P-lab ...
Tomato LeAGP-1 is a plasma membrane-bound
Tomato LeAGP-1 is a plasma membrane-bound

... Arabinogalactan-proteins (AGPs) are a class of highly glycosylated, hydroxyproline-rich glycoproteins that function in plant growth and development. Tomato LeAGP-1 represents a major AGP expressed in cultured cells and plants. Based on cDNA and amino acid sequence analyses along with carbohydrate an ...
Identification of the factors that interact with NCBP, an 80 kDa
Identification of the factors that interact with NCBP, an 80 kDa

... In this respect it is noteworthy that some tryptophan residues in eIF-4E, conserved among species, are important for cap binding activity (3), whereas no similar sequence is found in either NCBP or NIP1. Although essential domains of NCBP and NIP1 for cap binding activity remain to be elucidated, it ...
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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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