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Proteinas Efectoras De Genes
- 1. PROTEÍNAS Macromoléculas efectoras de la acción de los genes
- 37. NOMENCLATURA Resto de cada a.a : terminación en il Último residuo ( C terminal) : nombre completo del aminoñacido Ej: Serina, ácido aspártico, tirosina, lisina, alanina y cisteína Nombre: seril-aspartil-tirosil-lisil-alanil-cisteína.
- 38. Péptidos de importancia biológica Glutatión: Tripéptido (ácido glutámico, cisteína y glicina) Participa en sistema enzimático de oxidación y reducción. Previene daños oxidativos. Otros: Hormonas o factores liberadores Encefalinas Antibióticos
- 39. PROTEÍNAS Propiedades ácido – base Carga eléctrica depende de ionización de grupos en cadenas laterales Residuo lisina, arginina o histidina: carácter básico
- 40. Residuos de aspartato y glutamato: carácter ácido Grupo fenolico (tirosina) y sulfihidrilo (cisteína): débilmente ácido Tirosina Cisteína Proteínas: Capacidad amortiguadora o buffer por captar o liberar protones de acuerdo a concentración de H+
Notas del editor
- Numbering conventions for amino acids. In traditional names, the carbon atoms adjacent to the carboxyl group are identified by the Greek letters , , , etc. In the official IUPAC/IUBMB chemical names or systematic names, the carbon atom in the carboxyl group is number 1 and the adjacent carbons are numbered sequentially. Thus, the atom in traditional names is the carbon 2 atom in systematic names.
- Figure 3.1 Two representations of an L-amino acid at neutral pH. (a) General structure. An amino acid has a carboxylate group (whose carbon atom is designated C-1), an amino group, a hydrogen atom, and a side chain (or R group), all attached to C-2 (the -carbon). Solid wedges indicate bonds above the plane of the paper; dashed wedges indicate bonds below the plane of the paper. The blunt ends of wedges are nearer the viewer than the pointed ends. (b) Ball-and-stick model of serine (whose R group is —CH 2 OH). Note the alternative numbering and lettering systems for the carbon atoms.
- Numbering conventions for amino acids. In traditional names, the carbon atoms adjacent to the carboxyl group are identified by the Greek letters , , , etc. In the official IUPAC/IUBMB chemical names or systematic names, the carbon atom in the carboxyl group is number 1 and the adjacent carbons are numbered sequentially. Thus, the atom in traditional names is the carbon 2 atom in systematic names.
- Figure 3.1 Two representations of an L-amino acid at neutral pH. (a) General structure. An amino acid has a carboxylate group (whose carbon atom is designated C-1), an amino group, a hydrogen atom, and a side chain (or R group), all attached to C-2 (the -carbon). Solid wedges indicate bonds above the plane of the paper; dashed wedges indicate bonds below the plane of the paper. The blunt ends of wedges are nearer the viewer than the pointed ends. (b) Ball-and-stick model of serine (whose R group is —CH 2 OH). Note the alternative numbering and lettering systems for the carbon atoms.
- Figure 3.1 Two representations of an L-amino acid at neutral pH. (a) General structure. An amino acid has a carboxylate group (whose carbon atom is designated C-1), an amino group, a hydrogen atom, and a side chain (or R group), all attached to C-2 (the -carbon). Solid wedges indicate bonds above the plane of the paper; dashed wedges indicate bonds below the plane of the paper. The blunt ends of wedges are nearer the viewer than the pointed ends. (b) Ball-and-stick model of serine (whose R group is —CH 2 OH). Note the alternative numbering and lettering systems for the carbon atoms.
- Figure 3.2 Mirror-image pairs of amino acids. (a) Ball-and-stick models of L -serine and D -serine. Note that the two molecules are not identical; they cannot be superimposed. (b) L -Serine and D -serine.
- Figure 3.2 Mirror-image pairs of amino acids. (a) Ball-and-stick models of L -serine and D -serine. Note that the two molecules are not identical; they cannot be superimposed. (b) L -Serine and D -serine.
- Figure 3.2 Mirror-image pairs of amino acids. (a) Ball-and-stick models of L -serine and D -serine. Note that the two molecules are not identical; they cannot be superimposed. (b) L -Serine and D -serine.
- Assignment of configuration by the RS system. (a) Each group attached to a chiral carbon is assigned a priority based on atomic mass, 4 being the lowest priority. (b) By orienting the molecule with the priority 4 group pointing away (behind the chiral carbon) and tracing the path from the highest priority group to the lowest, the absolute configuration can be established. If the sequence 1, 2, 3 is clockwise, the configuration is R . If the sequence 1, 2, 3 is counterclockwise, the configuration is S . L -Serine has the S configuration.
- Assignment of configuration by the RS system. (a) Each group attached to a chiral carbon is assigned a priority based on atomic mass, 4 being the lowest priority. (b) By orienting the molecule with the priority 4 group pointing away (behind the chiral carbon) and tracing the path from the highest priority group to the lowest, the absolute configuration can be established. If the sequence 1, 2, 3 is clockwise, the configuration is R . If the sequence 1, 2, 3 is counterclockwise, the configuration is S . L-Serine has the S configuration.
- Assignment of configuration by the RS system. (a) Each group attached to a chiral carbon is assigned a priority based on atomic mass, 4 being the lowest priority. (b) By orienting the molecule with the priority 4 group pointing away (behind the chiral carbon) and tracing the path from the highest priority group to the lowest, the absolute configuration can be established. If the sequence 1, 2, 3 is clockwise, the configuration is R . If the sequence 1, 2, 3 is counterclockwise, the configuration is S . L-Serine has the S configuration.
- Aliphatic R Groups
- Figure 3.3 Stereoisomers of isoleucine.
- Figure 3.4 Formation of cystine. When oxidation links the sulfhydryl groups of two cysteine molecules, the resulting compound is a disulfide called cystine.
- Figure 3.5 Compounds derived from common amino acids. (a) -Aminobutyrate a derivative of glutamate. (b) Histamine, a derivative of histidine. (c) Epinephrine, a derivative of tyrosine. (d) Thyroxine and triiodothyronine, derivatives of tyrosine. Thyroxine contains one more atom of iodine (in parentheses) than does triiodothyronine.
- Figure 3.5 Compounds derived from common amino acids. (a) -Aminobutyrate a derivative of glutamate. (b) Histamine, a derivative of histidine. (c) Epinephrine, a derivative of tyrosine. (d) Thyroxine and triiodothyronine, derivatives of tyrosine. Thyroxine contains one more atom of iodine (in parentheses) than does triiodothyronine.
- Figure 3.5 Compounds derived from common amino acids. (a) -Aminobutyrate a derivative of glutamate. (b) Histamine, a derivative of histidine. (c) Epinephrine, a derivative of tyrosine. (d) Thyroxine and triiodothyronine, derivatives of tyrosine. Thyroxine contains one more atom of iodine (in parentheses) than does triiodothyronine.
- Figure 3.5 Compounds derived from common amino acids. (a) -Aminobutyrate a derivative of glutamate. (b) Histamine, a derivative of histidine. (c) Epinephrine, a derivative of tyrosine. (d) Thyroxine and triiodothyronine, derivatives of tyrosine. Thyroxine contains one more atom of iodine (in parentheses) than does triiodothyronine.
- Figure 3.5 Compounds derived from common amino acids. (a) -Aminobutyrate a derivative of glutamate. (b) Histamine, a derivative of histidine. (c) Epinephrine, a derivative of tyrosine. (d) Thyroxine and triiodothyronine, derivatives of tyrosine. Thyroxine contains one more atom of iodine (in parentheses) than does triiodothyronine.
- Figure 3.6 Titration curve for alanine. The first p K a value is 2.4; the second is 9.9. pI Ala represents the isoelectric point of alanine.
- Figure 3.7 Ionization of histidine. (a) Titration curve for histidine. The three p K a values are 1.8, 6.0, and 9.3. pI His represents the isoelectric point of histidine. (b) Deprotonation of the imidazolium ring of the side chain of histidine.
- Figure 3.7 Ionization of histidine. (a) Titration curve for histidine. The three p K a values are 1.8, 6.0, and 9.3. pI His represents the isoelectric point of histidine. (b) Deprotonation of the imidazolium ring of the side chain of histidine.
- Figure 3.8 Ionization of amino acid side chains. (a) Ionization of the protonated -carboxyl group of glutamate. The negative charge of the carboxylate anion is delocalized. (b) Deprotonation of the guanidinium group of the side chain of arginine. The positive charge is delocalized.
- Figure 3.8 Ionization of amino acid side chains. (a) Ionization of the protonated -carboxyl group of glutamate. The negative charge of the carboxylate anion is delocalized. (b) Deprotonation of the guanidinium group of the side chain of arginine. The positive charge is delocalized.
- Figure 3.9 Peptide bond between two amino acids. The structure of the peptide linkage can be viewed as the product of a condensation reaction in which the -carboxyl group of one amino acid condenses with the -amino group of another amino acid. The result is a dipeptide in which the amino acids are linked by a peptide bond. Here, alanine is condensed with serine to form alanylserine.
- Figure 4.41 Scanning electron micrograph of mammalian erythrocytes. Each cell contains approximately 300 million hemoglobin molecules.
- Figure 4.42 Human (Homo sapiens) oxyhemoglobin. (a) Structure of human oxyhemoglobin showing two and two subunits. Heme groups are shown as stick models. [PDB 1 HND]. (b) Schematic diagram of the hemoglobin tetramer. The heme groups are red.
- Figure 4.42 Human (Homo sapiens) oxyhemoglobin. (a) Structure of human oxyhemoglobin showing two and two subunits. Heme groups are shown as stick models. [PDB 1 HND]. (b) Schematic diagram of the hemoglobin tetramer. The heme groups are red.
- Figure 4.42 Human (Homo sapiens) oxyhemoglobin. (a) Structure of human oxyhemoglobin showing two and two subunits. Heme groups are shown as stick models. [PDB 1 HND]. (b) Schematic diagram of the hemoglobin tetramer. The heme groups are red.