'2 binding' diaporamas de présentation

Protein Function/Enzyme Regulation/Biosignalling

Protein Function/Enzyme Regulation/Biosignalling. Chpts. 5, 6, 12. 1 o , 2 o , 3 o , 4 o Structures REMEMBER??. Structure defines function If >1 polypeptide chain, 4 o structure Chains not independent Book: Proteins are dynamic structures. Definitions (Chpt. 5).

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Protein Function/Enzyme Regulation/Biosignalling

Protein Function/Enzyme Regulation/Biosignalling. Chpts. 5, 6, 12. 1 o , 2 o , 3 o , 4 o Structures REMEMBER??. Structure defines function If >1 polypeptide chain, 4 o structure Chains not independent Book: Proteins are dynamic structures. Definitions (Chpt. 5).

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Proteins are not rigid structures: Protein dynamics, conformational variability,

Proteins are not rigid structures: Protein dynamics, conformational variability, and thermodynamic stability. Dr. Andrew Lee UNC School of Pharmacy (Div. Chemical Biology and Medicinal Chemistry) UNC Med School (Biochemistry and Biophysics). drewlee@unc.edu 201A Beard Hall.

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Something Cool

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Protein Structures

Protein Structures. Primary structure Amino acid sequence Edman degradation, MS, deduce from DNA Secondary structure Recurring structural pattern Circular dichroism (CD, ???????? ) Tertiary structure 3D folding of a polypeptide chain X-ray crystallography, NMR Quaternary structure

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Protein Function

Protein Function. Protoporphyrin. Heme. Spacefill representation of heme. Iron in Mb-bound heme can not be oxidized. Myoglobin. Ligand binding to heme. Mb increases the selectivity of O 2 binding. Ligand binding equilibrium. O 2 binding by Mb. Hb subunits are homologous to Mb.

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Molecules, Gene and disease Session 2 Lecture 4 Oxygen transport proteins

Molecules, Gene and disease Session 2 Lecture 4 Oxygen transport proteins. Transport of O 2 and CO 2 by hemoglobin. Haemoglobin and Myoglobin. MYOGLOBIN. 153 amino acids (18 KDa) O 2 -carrying protein in muscle Contains essential prosthetic group (haem: contains Fe atom)

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Structures of Myoglobin and Hemoglobin

Structures of Myoglobin and Hemoglobin. Myoglobin ( Mb ) - monomeric protein that facilitates the diffusion of oxygen in vertebrates Hemoglobin ( Hb ) - tetrameric protein that carries oxygen in the blood

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Structures of Myoglobin and Hemoglobin

Structures of Myoglobin and Hemoglobin. Myoglobin ( Mb ) - monomeric protein that facilitates the diffusion of oxygen in vertebrates Hemoglobin ( Hb ) - tetrameric protein that carries oxygen in the blood

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Chapter 5.1: Protein Function - Reversible Binding of Protein to a Ligand

Chapter 5.1: Protein Function - Reversible Binding of Protein to a Ligand. CHEM 7784 Biochemistry Professor Bensley. CHAPTER 5.1 Reversible Binding of Protein to a Ligand. Reversible binding of ligands Structure of myoglobin and hemoglobin Origin of cooperativity in hemoglobin.

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Protein Function

Protein Function. Function relies on interactions with other molecules Binding of molecules to proteins is reversible Ligand = Binding site =. HIV protease + drug inhibitor. Protein Function. Function relies on interactions with other molecules

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Chapter 5

Chapter 5. Chem 341 Suroviec Fall 2013. I. Introduction. Every protein has a unique 3-D structure. II. Myoglobin. Small intercellular protein. A. Heme group. Heme contains 4 pyrrole groups

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Chapter 4 (part 3)

Chapter 4 (part 3). 3-D Structure / Function. Animal Scrapie : sheep TME (transmissible mink encephalopathy): mink CWD (chronic wasting disease): muledeer, elk BSE (bovine spongiform encephalopathy): cows Human CJD : Creutzfeld-Jacob Disease FFI : Fatal familial Insomnia Kuru.

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Protein Function

Protein Function. Hemoglobin as a model systems for: Ligand binding Quaternary structure and symmetry Cooperative behavior Allosteric conformational effects Genetic variation, selection, disease. Myoglobin (a monomeric form of hemoglobin).

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Oxygen Storage in Muscle Tissue

Myoglobin (Mb) Originally isolated from sperm whales 10X abundance greater in aquatic- than terrestrial-mammals Mb knockout mice exhibit normal exercise capacity Detoxification of reactive nitric oxide a signaling molecule. Oxygen Storage in Muscle Tissue.

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Hemoglobin (haemoglobin, Hb, Hgb)

Hemoglobin (haemoglobin, Hb, Hgb). red cells in blood carry O 2 from lung to tissues by hemoglobin, a 4-subunit protein having an O 2 -binding prosthetic group, heme, that gives blood its color (Hb also carries (some) CO 2 and H + back to the lung)

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Chap. 5A Protein Function

Chap. 5A Protein Function. Topics Reversible Binding of a Protein to a Ligand: Oxygen-binding Proteins. The heme group Myoglobin Hemoglobin Sickle-cell Anemia. Fig. 5-19. Normal (a) and sickle-cell anemia (b) erythrocytes. Intro. to Ligand-binding Proteins.

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CHMI 2227E Biochemistry I

CHMI 2227E Biochemistry I. Proteins: Quaternary structure. Quaternary structure. hydrophobic. hydrophilic. Porin: a trimeric membrane-bound protein. Quaternary structure. Quaternary structure Hemoglobin. HbA. Myoglobin. Quaternary structure Hemoglobin HbA vs myoglobin.

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CHMI 2227E Biochemistry I

CHMI 2227E Biochemistry I. Proteins: Quaternary structure. Quaternary structure. Quaternary structure involves several polypeptides: Oligomers Heteromers

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Suggested HW Ch. 5

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