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Study Questions for Chapter 1 – The Cell
Study Questions for Chapter 1 – The Cell

... maximal rate (Vmax) and cannot operate any faster. The substrate concentration that results in the  enzyme functioning at ½ its the maximal rate is called the Km. Km can be considered an index of the  affinity an enzyme has for its substrate – a high Km indicates low affinity (i.e., it takes a lot o ...
CRACKING THE GENETIC CODE
CRACKING THE GENETIC CODE

... Assay developed by Marshall Nirenberg and his collaborators for deciphering the genetic code. They prepared 20 E. coli extracts containing all the aminoacyl-tRNAs (tRNAs with amino acid attached). In each extract sample, a different amino acid was radioactively labeled (green); the other 19 amino ac ...
Chapter 04 - Lecture Outline
Chapter 04 - Lecture Outline

... Introduction: Because enzymes regulate metabolic pathways that allow cells to survive, cells must have the information for producing these special proteins. Recall from Chapter 2, that in addition to enzymes, proteins have several important functions in cells, including structure (keratin), transpor ...
Chapter 13 Lecture Notes: Peptides, Proteins
Chapter 13 Lecture Notes: Peptides, Proteins

... 10. Compare and contrast peptides and proteins. 11. Understand and define primary, secondary, tertiary, and quaternary protein structure. Name the noncovalent interactions that are responsible for each level of structure. 12. Explain what is meant by the term denaturatio and list the ways to denatur ...
BME205H1_20171_621493426054BME205
BME205H1_20171_621493426054BME205

... the other tripeptides, at least one of the amino acids belongs to the nonpolar charged class [1 mark]. 7. [7 marks] Alpha-5 integrin is a single pass transmembrane receptor protein, which means that only one segment of the protein is embedded in the plasma membrane of the cell. The part of the prote ...
Biochemistry I, Spring Term 2001 - Second Exam answer key
Biochemistry I, Spring Term 2001 - Second Exam answer key

... peptides containing Methionine (side chain: -C-C-S-CH3). Sketch your modification below and briefly support your answer with explicit reference to the molecular forces that would be involved in the recognition of the Methionine. ALTERNATIVELY you can discuss how you might modify HIV proteases inhibi ...
CHAPTER 4: CELLULAR METABOLISM
CHAPTER 4: CELLULAR METABOLISM

... Introduction: Because enzymes regulate metabolic pathways that allow cells to survive, cells must have the information for producing these special proteins. Recall from Chapter 2, that in addition to enzymes, proteins have several important functions in cells, including structure (keratin), transpor ...
2.5 | Four Types of Biological Molecules
2.5 | Four Types of Biological Molecules

... causes digestive discomfort. Sugars may also be linked together to form small chains called oligosaccharides (oligo 5 few). Most often such chains are found covalently attached to lipids and proteins, converting them into glycolipids and glycoproteins, respectively. Oligosaccharides are particularly ...
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 ...
Cellular Membranes Reading Assignments
Cellular Membranes Reading Assignments

... Interactions of Integral Membrane Proteins EXTRACELLULAR SIDE N-terminus ...
Mitochondria
Mitochondria

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Proteins in Serum and Urine - Ústav lékařské biochemie a

... inflammation, tissue injury due to trauma or surgery, or tumor proliferation. In many other situations the reaction is present in a less pronounced form, such as the condition following an extreme physical exercise, acute heart stroke or around delivery. Simply stated, the acute phase reaction is tr ...
Chapter 1: Prelude
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... rotate due to ist partial double-bond character. The rigidity enables proteins to have well-defined threedimensional forms. The folding of proteins is made possible by free rotation on either side of the peptide unit.  Helix and  pleated Sheet The-helix is stabilized by hydrogen bonds between th ...
function finders
function finders

... -- Each P53 molecule has three regions: one binds to other P53 molecules, one switches genes on and one binds to DNA. -- P53 has several anti-cancer properties: it can activate DNA repair proteins when DNA has been damaged; it can suspend cell division, allowing time for damaged DNA to be repaired; ...
INTRODUCTORY BIOCHEMISTRY Bio. 28 First Midterm
INTRODUCTORY BIOCHEMISTRY Bio. 28 First Midterm

... fall very close to the straight line implies (choose one): a) The enzyme does not exhibit cooperative substrate binding. b) There is no competitive inhibitor present. c) The enzyme has a high catalytic efficiency. d) The enzyme has a constant Vmax. ...
Predicting functional linkages from gene fusions with
Predicting functional linkages from gene fusions with

... topoisomerase proteins, are linked due to the presence of the yeast topoisomeraseII (Top2) protein, which is a fusion of both gyrase A-like and gyrase B-like domains. To apply orthology to predict precise linkages between these proteins, the fusion protein must first be separated into domains, and t ...
Biochimica et Biophysica Acta
Biochimica et Biophysica Acta

... scanning of stained gels [18]. Amino acid analyses were carried out as described [24]. The amounts of serine and threonine were extrapolated to zero time using values of 90 and 95%, respectively, for a hydrolysis time of 24 h. The N H 2-terminal amino acid was determined by the dansyl procedure [25] ...
Classification of amino acids: -
Classification of amino acids: -

... 3. Basic: this class contain only 3 standard amino acids: (His, Lys, Arg).  20 amino acids called “Standard amino acids” occur in almost all proteins & are coded in the DNA.  Some amino acids may become chemically modified after being assembled in proteins, which called the unusual L – α amino aci ...
best
best

... The larger leucine sidechain must not quite fit in the core as well as the valine, disrupting van der Waals interactions (3 pts) Thr: The enthalpy is higher, therefore, more interactions have to be broken during unfolding (2 pts) The OH group on the Threonine can form a hydrogen bond to either a mai ...
Forces Produced by Protofilament Curls Nucleotide Preference for End Binding Proteins
Forces Produced by Protofilament Curls Nucleotide Preference for End Binding Proteins

... •  GTPγS  microtubules  had  brighter  tips   than  GTP  microtubules   •  EB3  showed  the  greatest  binding  affinity   at  the  tip  for  both  microtubule  types   •  EB2  showed  the  greatest  binding  affinity   for    GTPγS  microtubul ...
Searching for Genes
Searching for Genes

... All branches on the tree of life share common roots. One way to study those roots is to look to DNA sequences. So, when the Roberts lab began studying the evolution of cellulose synthesis, one place they looked was at the available DNA sequence information. Even now, as they expand their studies to ...
best
best

... The larger leucine sidechain must not quite fit in the core as well as the valine, disrupting van der Waals interactions (3 pts) Thr: The enthalpy is higher, therefore, more interactions have to be broken during unfolding (2 pts) The OH group on the Threonine can form a hydrogen bond to either a mai ...
Concept 3.1 Nucleic Acids Are Informational
Concept 3.1 Nucleic Acids Are Informational

... activation energy and speed a reaction. – The active site orients substrates in the correct orientation for the reaction. – As the active site binds the substrate, it may put stress on bonds that must be broken, making it easier to reach the transition state. – R groups at the active site may create ...
Introduction and Review
Introduction and Review

... Panel 2–1 Chemical bonds and groups Panel 2–2 The chemical properties of water Panel 2–3 An outline of some of the types of sugar Panel 2–4 Fatty acids and other lipids Panel 2–5 The 20 amino acids found in proteins Panel 2–6 A survey of the nucleotides Panel 2–7 The principal types of weak noncoval ...
Nickel Affinity Chromatography Protocol/Guide
Nickel Affinity Chromatography Protocol/Guide

... Theory and Introduction: Ni-Affinity Chromatography uses the ability of His to bind nickel. Six histadine amino acids at the end of a protein (either N or C terminus) is known as a 6X His tag. Nickel is bound to an agarose bead by chelation using nitroloacetic acid (NTA) beads. Several companies pro ...
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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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