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Chapter 1--Title
Chapter 1--Title

... These local conformations are specified in terms of regular folding patterns such as helices, pleated sheets, and turns ...
E. coli - Department of Chemistry
E. coli - Department of Chemistry

... pseudochiral center ...
Mitochondrial Lab - University of Colorado Denver
Mitochondrial Lab - University of Colorado Denver

... Competitive Inhibitors resemble the normal substrate -but cannot be turned into product—so they tie up enzymes by binding to their active site. Malonate is a molecule that looks like succinate, but it cannot be made into fumaric acid (product) so malonate is a competitive inhibitor. Malonate is in ...
BCHM 463 Supplemental Problems for Friday, April 2, 2004 1. Write
BCHM 463 Supplemental Problems for Friday, April 2, 2004 1. Write

... organisms and also occasionally requires 2,3-BPG as a cofactor to reactivate the enzyme if it becomes dephosphorylated. Recall that 2,3-BPG is an allosteric modulator of hemoglobin in erythrocytes although the 2,3-BPG produced by escape from phosphoglycerate mutase is neglible. This of course means ...
Protein structure and function
Protein structure and function

Translation Activity - SeaWorld/Busch Gardens ANIMALS
Translation Activity - SeaWorld/Busch Gardens ANIMALS

... protein their group represents by observing the polymer of amino acids and correlating them to the specific protein they code for. This can be accomplished by utilizing the Protein table. Additionally, students should define the protein type they represent. I.E. How does the animal utilize that part ...
An intersubunit lock-and-key `Clasp` motif in the dimer interface of
An intersubunit lock-and-key `Clasp` motif in the dimer interface of

Controlling reaction specificity in pyridoxal phosphate
Controlling reaction specificity in pyridoxal phosphate

... common step in all pyridoxal phosphate catalyzed reactions is the formation of an external aldimine intermediate with the substrate. This occurs through a series of steps in which the unprotonated amino group of the substrate attacks the protonated Schiff base formed between a lysine side chain in t ...


... mainchain and sidechain Quaternary: Structure/arrangement of multiple Y-shaped molecule. Heavy and light chains held chains together by disulfide bonds. B6: i) The secondary structure is β-strand. ii) Surface, since there are polar residues on one side of the strand and non-polar residues on the oth ...
CHEM 527 Final exam, Fall 2006 NAME
CHEM 527 Final exam, Fall 2006 NAME

Summary
Summary

... 123, they also derive from similar secondary structural elements. Interestingly, the two pairs of leucines deriving from the positionally related helix of SMOA and three stranded antiparallel sheet of PHBH are still in close proximity and pointing in roughly the same direction. ...
Final Examination
Final Examination

Step 1 - Template Recognition and Initial Alignment
Step 1 - Template Recognition and Initial Alignment

... the web, selects the PDB as database to search, wait 5 seconds, and obtains a list of hits the modeling templates and corresponding alignments. Usually, the hit with most sequence identity will be the first option, see figure 2, but one should keep in mind other points of interest, for example activ ...
REVIEW OF FRESHMAN CHEMISTRY: pH, pK, buffers, Henderson
REVIEW OF FRESHMAN CHEMISTRY: pH, pK, buffers, Henderson

... of a specific His residue (say it's residue #20 in the amino acid sequence of that protein) in the uncharged (neutral) form at pH 4.5. What is the pKa of that specific His residue in that protein? (You need to know the ionization properties of the functional group of His to answer this question -loo ...
Lecture 2: Introduction to Proteins
Lecture 2: Introduction to Proteins

... base as in the form of the acid when the pH is 1 unit above the pKa.) B. At pH 5.0, the COOH/COO– ratio is 10/1. We can do this problem most simply by using proportions; the total of the carboxyl group is COOH + COO– = 10 + 1 = 11. The fraction of the total in the form of the acid (COOH) is (COOH) / ...
AP Biology
AP Biology

... activation energy & speed up reaction ...
ADP-ribosyltransferases: plastic tools for inactivating protein and
ADP-ribosyltransferases: plastic tools for inactivating protein and

Crystal Structure of 4-Chlorobenzoate:CoA Ligase/Synthetase in the
Crystal Structure of 4-Chlorobenzoate:CoA Ligase/Synthetase in the

Access Slides - Science Signaling
Access Slides - Science Signaling

... SREBP transport. SREBP exists in a hairpinlike conformation with a small luminal loop and two large cytoplasmic domains. The NH2terminal domain is a basic helix-loop-helix (bHLH) transcription factor and the COOHterminal domain is a regulatory factor (REG) that binds SCAP. When cells are loaded with ...
Polymer - Deans Community High School
Polymer - Deans Community High School

... All proteins contain the elements C,N,O,H. They are condensation polymers, made by amino acids linking together. An amine group of one molecule links to the carboxyl group of another molecule to form an amide or peptide bond. The body makes specific proteins it needs, but cannot make all the amino a ...
Amino acids degradation and synthesis
Amino acids degradation and synthesis

... when fatty acids are broken down for energy in the liver and kidney. The three ketone bodies are acetone, acetoacetic acid and beta-hydroxybutyric acid. Ketone bodies are transported from the liver to other tissues, where acetoacetate and beta-hydroxybutyrate can be reconverted to acetyl-CoA to prod ...
Enzymes - WordPress.com
Enzymes - WordPress.com

... another, thus changing the oxidation state of both substrates • In many oxidation reduction reactions, hydrogen is transferred along with electrons • In other reactions, a molecule or atom of oxygen could be transferred to a substance; electrons could also be transferred to oxygen 2. Transferases • ...
elisa - WordPress.com
elisa - WordPress.com

... or substance that undergoes change. – Substrates bind to active sites on the surface of enzymes and are converted or changed. In ELISA the specific substrate used changes color. – Substrate Solution: • chromogen A and • chromogen B should be mixed together in equal volumes up to 15 minutes before us ...
Enzyme Catalysis Lab
Enzyme Catalysis Lab

Measurement of Enzymes and Their Clinical Significance
Measurement of Enzymes and Their Clinical Significance

... Enzymes • Using Enzyme Mass – Measure protein mass NOT catalytic activity ...
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Catalytic triad



A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.
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