Peptide in a sentence
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(1) Thymosin is a peptide hormone.
(2) The peptide bond is a covalent bond.
(3) Melittin is a peptide found in bee venom.
(4) Adrenocorticotropic is a peptide hormone.
(5) Angiotensin I is a 10-amino acid peptide.
(6) The peptide bond is resistant to hydrolysis.
(7) The peptide was acetylated by the acetyl group.
(8) Dynorphin acts as an endogenous opioid peptide.
(9) Chymotrypsin cleaves peptide bonds in proteins.
(10) Enkephalin is a peptide composed of amino acids.
Peptide sentence
(11) The peptide bond is resistant to acid hydrolysis.
(12) The peptide was cleavable by proteolytic enzymes.
(13) Adrenocorticotrophic hormone is a peptide hormone.
(14) The peptide is phosphorylated by a protein kinase.
(15) Chymotrypsin hydrolyzes peptide bonds in proteins.
(16) The peptide bond was cleavable by acid hydrolysis.
(17) The peptide bond is highly resistant to hydrolysis.
(18) The tryptic peptide bond was cleaved using trypsin.
(19) Amino acids can form peptide bonds with each other.
(20) The ribosome is the site of peptide bond formation.
Peptide make sentence
(21) The function of trypsins is to cleave peptide bonds.
(22) Hirudin is a peptide found in the saliva of leeches.
(23) Use aminopeptidase to cleave specific peptide bonds.
(24) Melanocyte-stimulating hormone is a peptide hormone.
(25) Amanitin is a cyclic peptide with a unique structure.
(26) The enzyme catalyzed the formation of a peptide bond.
(27) Aprotic solvents are often used in peptide synthesis.
(28) The peptide bond plays a key role in protein folding.
(29) Oligopeptides are commonly used in peptide synthesis.
(30) Tryptic digestion produces smaller peptide fragments.
Sentence of peptide
(31) The enzyme catalysed the formation of a peptide bond.
(32) This protein catalyzes the formation of peptide bonds.
(33) Acyls are important in the formation of peptide bonds.
(34) The enzyme catalysed the cleavage of the peptide bond.
(35) The peptide oligomerizes to form a bioactive molecule.
(36) The peptide bond can be cleaved by enzymatic reactions.
(37) Cleavable peptides are often used in peptide synthesis.
(38) Peptise is involved in the hydrolysis of peptide bonds.
(39) Acylating reagents are often used in peptide synthesis.
(40) Amidogens can be used as reagents in peptide synthesis.
Peptide meaningful sentence
(41) Dipeptides can be formed through peptide bond formation.
(42) The peptide bond is a crucial link in protein synthesis.
(43) The peptide bond is a key feature of polypeptide chains.
(44) The polypeptide chain is held together by peptide bonds.
(45) Glucagon is a peptide hormone composed of 29 amino acids.
(46) Amino acid residues are linked together by peptide bonds.
(47) The peptide bond is formed through a nucleophilic attack.
(48) Angiotensin I is a peptide hormone produced by the liver.
(49) Secretin is a peptide hormone composed of 27 amino acids.
(50) Phalloidin is a toxic peptide found in certain mushrooms.
Peptide sentence examples
(51) Peptide synthesis is a process of forming a peptide bond.
(52) The protease cleaves the peptide bond between amino acids.
(53) The peptide bond is stable under physiological conditions.
(54) The peptide bond is essential for the folding of proteins.
(55) The peptide bond is characterized by its planar structure.
(56) The peptide bond is a key determinant of protein function.
(57) The peptide undergoes phosphorylation by a protein kinase.
(58) The peptide bond is susceptible to chemical modifications.
(59) Gly is often used as a building block in peptide synthesis.
(60) Calcitonin is a peptide hormone composed of 32 amino acids.
Sentence with peptide
(61) The peptide bond is formed through a condensation reaction.
(62) The cleavable peptide can be easily broken down by enzymes.
(63) Nisin is a peptide produced by certain strains of bacteria.
(64) The tryptic process involves the cleavage of peptide bonds.
(65) The enzyme hydrolyses the peptide bond between amino acids.
(66) Oligopeptides are often used in peptide mapping techniques.
(67) The octapeptide is a peptide composed of eight amino acids.
(68) The tryptic peptide was identified using mass spectrometry.
(69) The peptide was acetylated by the acetyltransferase enzyme.
(70) Peptides are chains of amino acids linked by peptide bonds.
Use peptide in a sentence
(71) Peptide hormones can act as signaling molecules in the body.
(72) Peptide hormones are produced by various glands in the body.
(73) The peptide bond is formed in a ribosome-catalyzed reaction.
(74) The radiolabelled peptide was used to study protein folding.
(75) Anticodons are essential for the formation of peptide bonds.
(76) Dipeptides can serve as precursors for larger peptide chains.
(77) The peptide bond is a fundamental building block of proteins.
(78) Pentagastrin is a synthetic peptide used in medical research.
(79) Cecropin is a type of antimicrobial peptide found in insects.
(80) The peptide bond is a crucial component of protein structure.
Sentence using peptide
(81) The peptide bond is crucial for protein-protein interactions.
(82) The high pH is catalysing the hydrolysis of the peptide bond.
(83) Peptise is an enzyme that specifically targets peptide bonds.
(84) The glycyl group is often involved in peptide bond formation.
(85) Guanidine is commonly used as a reagent in peptide synthesis.
(86) Amanitin is a cyclic peptide that binds to RNA polymerase II.
(87) The amidin compound is a common reagent in peptide synthesis.
(88) Motilin is a peptide hormone that consists of 22 amino acids.
(89) The circularized peptide showed increased stability in serum.
(90) Vasopressin is a peptide hormone composed of nine amino acids.
Peptide example sentence
(91) Trypsin cleaves peptide bonds at specific amino acid residues.
(92) Peptide arrays are used to study protein-protein interactions.
(93) The peptide bond is formed during translation in the ribosome.
(94) The peptide bond is formed by the removal of a water molecule.
(95) Aprotic solvents are often used in peptide coupling reactions.
(96) Acetonitrile is often used as a solvent for peptide synthesis.
(97) Acyls are often used as acylating agents in peptide synthesis.
(98) Amides are often used as coupling agents in peptide synthesis.
(99) The amino group is involved in the formation of peptide bonds.
(100) Acylates play a crucial role in the formation of peptide bonds.
Sentence with word peptide
(101) The dimerization of the peptide was essential for its function.
(102) Peptide hormones can bind to specific receptors on target cells.
(103) The peptide bond is highly conserved across different organisms.
(104) Thyrocalcitonin is a peptide hormone composed of 32 amino acids.
(105) Tripeptide synthesis is a common technique in peptide chemistry.
(106) Acetylating a peptide can protect it from enzymatic degradation.
(107) Hydrolyses of proteins result in the breakdown of peptide bonds.
(108) Peptide-based imaging agents can be used for diagnostic purposes.
(109) The dipeptide was used as a building block for peptide synthesis.
(110) The peptide bond is formed by the action of peptidyl transferase.
Sentence of peptide
(111) The peptide bond is a key target for drug design and development.
(112) Proinsulin is cleaved into insulin and C peptide during secretion.
(113) Angiotensin I is a peptide hormone that acts as a vasoconstrictor.
(114) The carboxyl group is important in the formation of peptide bonds.
(115) The peptide bond is formed by the condensation of two amino acids.
(116) The cecropin peptide is part of the insect's innate immune system.
(117) The dipeptide was synthesized using solid-phase peptide synthesis.
(118) Bombesin is a peptide hormone found in the gastrointestinal tract.
(119) The reaction hydrolyses the peptide bond in the polypeptide chain.
(120) The peptide sequence determines the specific function of a protein.
Peptide used in a sentence
(121) Peptide libraries are used to screen for potential drug candidates.
(122) The secondary structure of a peptide refers to its folding pattern.
(123) The peptide bond is formed through the release of a water molecule.
(124) The dipeptide was used as a template for peptide library synthesis.
(125) The main function of pepsin is to cleave peptide bonds in proteins.
(126) The peptide bond is planar due to the resonance of the amide group.
(127) The peptide bond is susceptible to enzymatic cleavage by proteases.
(128) Solid-phase peptide synthesis is a valuable tool in drug discovery.
(129) The alanyl residue is located at the N-terminus of a peptide chain.
(130) Bradykinin is a peptide that plays a role in inflammation and pain.
Peptide sentence in English
(131) Peptide phage display allows for identification of peptide ligands.
(132) Peptide engineering allows for customization of peptide properties.
(133) The enzyme's function is to hydrolyze the peptide bonds in proteins.
(134) The amino group is often involved in the formation of peptide bonds.
(135) Peptide-based inhibitors can block the activity of specific enzymes.
(136) The amido bond in this peptide is susceptible to enzymatic cleavage.
(137) Bacteriocin is a type of antimicrobial peptide produced by bacteria.
(138) The cecropin gene is responsible for producing the cecropin peptide.
(139) Formation of a peptide bond requires the interaction of amino acids.
(140) The peptide bond is formed by the ribosome during protein synthesis.
(141) Phalloidin is a toxic peptide found in certain species of mushrooms.
(142) Somatostatin is a cyclic peptide hormone composed of 14 amino acids.
(143) Amanitin is a cyclic peptide toxin that disrupts cellular processes.
(144) Trypsin is a serine protease that specifically cleaves peptide bonds.
(145) The structure of a peptide is formed by linking amino acids together.
(146) The formation of a peptide bond requires the presence of amino acids.
(147) The peptide bond is responsible for the linear structure of proteins.
(148) Aminolysis reactions can be used to cleave peptide bonds in proteins.
(149) Endopeptidases are enzymes that break peptide bonds within a protein.
(150) The peptide bond is relatively stable under physiological conditions.
(151) The peptide bond is characterized by a partial double bond character.
(152) Acyl phosphates can be used as acylating agents in peptide synthesis.
(153) Melittin is a fascinating peptide with diverse biological activities.
(154) The chemical reaction will hydrolyze the peptide bond in the protein.
(155) The peptide bond is responsible for the primary structure of proteins.
(156) The peptide bond is essential for the stability of protein structures.
(157) The peptide bond is responsible for the rigidity of protein backbones.
(158) The peptide bond is essential for the biological activity of proteins.
(159) The mechanism of action of proteinase involves cleaving peptide bonds.
(160) Acylates are commonly used as acylating reagents in peptide synthesis.
(161) Solid-phase peptide synthesis enables the creation of cyclic peptides.
(162) Enkephalin is a peptide that is produced in the brain and spinal cord.
(163) Endopeptidase is an enzyme that cleaves peptide bonds within a protein.
(164) The synthesis of pentapeptides requires expertise in peptide chemistry.
(165) The cecropin peptide has been shown to be non-toxic to mammalian cells.
(166) The peptide bond is formed through the elimination of a water molecule.
(167) Solid-phase peptide synthesis is a crucial step in protein engineering.
(168) Bradykinin is a peptide that plays a role in regulating blood pressure.
(169) The acylation of amino acids is an important step in peptide synthesis.
(170) The chylification of proteins involves the hydrolysis of peptide bonds.
(171) The proinsulin molecule consists of an A chain, B chain, and C-peptide.
(172) Kallikrein is an enzyme that cleaves specific peptide bonds in proteins.
(173) The peptide bond is formed through the interaction of functional groups.
(174) Aminolysis is an important tool in the synthesis of peptide-based drugs.
(175) Cleavable linkers are essential for the synthesis of peptide conjugates.
(176) Solid-phase peptide synthesis enables the creation of modified peptides.
(177) The protonation of the peptide backbone affects its secondary structure.
(178) Proinsulin is cleaved at specific sites to remove the C-peptide segment.
(179) The radiolabeled peptide was used to study protein-protein interactions.
(180) Natriuresis is regulated by hormones such as atrial natriuretic peptide.
(181) Peptide mass spectrometry is a powerful tool for peptide identification.
(182) Peptide hormones are chemical-messenger that are made up of amino acids.
(183) The n-methylated form of a peptide may have altered biological activity.
(184) The peptide bond is essential for the recognition and binding of ligands.
(185) The word pentapeptide refers to a peptide consisting of five amino acids.
(186) Scientists are investigating the mechanism of acylated peptide formation.
(187) The radiolabelled peptide was used to study protein-protein interactions.
(188) The octapeptide has been synthesized using solid-phase peptide synthesis.
(189) The dephosphorylated peptide was synthesized using solid-phase synthesis.
(190) Amino acids are linked together by peptide bonds to form a protein chain.
(191) The secretion of aldosterones is inhibited by atrial natriuretic peptide.
(192) Gramicidin is a cyclic peptide that is composed of two amino acid chains.
(193) Cholecystokinin is a peptide hormone found in the gastrointestinal system.
(194) Peptide-based nanoparticles have shown potential in drug delivery systems.
(195) The binding energy of a peptide bond is responsible for protein structure.
(196) The methyl group is often used as a protecting group in peptide synthesis.
(197) Fibrinopeptide is a peptide fragment derived from the fibrinogen molecule.
(198) The biuret test is sensitive to the presence of peptide bonds in proteins.
(199) The monosome catalyzes the formation of peptide bonds between amino acids.
(200) It is important to acylate the amino acid in order to form a peptide bond.
(201) Peptide synthesis can be achieved via solid-phase or liquid-phase methods.
(202) The bivalences of nitrogen atoms allow for the formation of peptide bonds.
(203) Bombesin is a peptide hormone that plays a role in regulating food intake.
(204) Solid-phase peptide synthesis involves the use of resin-bound amino acids.
(205) Kinin is a peptide that plays a crucial role in the inflammatory response.
(206) Cholecystokinin is a relatively small peptide consisting of 33 amino acids.
(207) The stability of a peptide can be influenced by its amino acid composition.
(208) Atrial natriuretic peptide is a hormone that helps regulate blood pressure.
(209) The function of proteolytic enzymes is to cleave peptide bonds in proteins.
(210) Pentapeptides can be used as building blocks for larger peptide structures.
(211) The tripeptide structure of this peptide is stabilized by hydrogen bonding.
(212) The cecropin peptide has shown promise in fighting drug-resistant bacteria.
(213) The study of epitopes has led to the development of peptide-based vaccines.
(214) Solid-phase peptide synthesis is a key method in the field of biochemistry.
(215) Pentagastrin is a synthetic peptide that stimulates gastric acid secretion.
(216) The ribosome has a catalytic center that facilitates peptide bond formation.
(217) The ethyl group is commonly used as a protecting group in peptide synthesis.
(218) Peptide hormones play a crucial role in regulating various bodily functions.
(219) The hormone atrial natriuretic peptide is involved in promoting natriuresis.
(220) Tyrocidine is a cyclic peptide that forms pores in bacterial cell membranes.
(221) Trypsinogen is converted to trypsin by the removal of a small peptide chain.
(222) Carboxypeptidase hydrolyzes peptide bonds at the C-terminal end of proteins.
(223) Amino acids are linked together by peptide bonds to form polypeptide chains.
(224) Peptide mimetics are compounds that mimic the structure of natural peptides.
(225) Peptide bonds are formed through a condensation reaction between amino acids.
(226) Oligopeptide synthesis can be achieved through solid-phase peptide synthesis.
(227) Exopeptidase is an enzyme that cleaves peptide bonds at the ends of proteins.
(228) Solid-phase peptide synthesis is a widely used method for producing peptides.
(229) The zwitterion form of an amino acid is essential for peptide bond formation.
(230) The synthetase enzyme plays a crucial role in the formation of peptide bonds.
(231) The n-methylated form of a peptide can enhance its stability and bioactivity.
(232) The process of linking amino acids together is called peptide bond formation.
(233) The hormone atrial natriuretic peptide plays a role in promoting natriuresis.
(234) Angiotensin I is a peptide that is produced in response to low blood pressure.
(235) Peptide therapeutics offer a targeted approach for treating specific diseases.
(236) Peptide drugs often have a shorter half-life compared to small molecule drugs.
(237) The array 'dipeptides' provides a comprehensive overview of peptide diversity.
(238) The specificity of endopeptidase determines which peptide bonds it can cleave.
(239) The peptide bond is crucial for the formation of secondary protein structures.
(240) Alanyl can form peptide bonds with other amino acids during protein synthesis.
(241) The function of rRNA is to catalyze peptide bond formation during translation.
(242) Angiotensin I is a peptide that is involved in the regulation of blood volume.
(243) Aminopeptidase, which is a serine protease, cleaves peptide bonds selectively.
(244) Hirudin, which is a peptide, is known for its ability to dissolve blood clots.
(245) The chemical reaction will hydrolyze the peptide bond in the protein molecule.
(246) The hydrolyzable amide bond in the peptide was cleaved by proteolytic enzymes.
(247) The lysate was digested with a specific protease to generate peptide fragments.
(248) The array 'dipeptides' enables the discovery of new peptide-based therapeutics.
(249) The amido bond in this peptide is responsible for its conformational stability.
(250) Thyrotropin-releasing hormone is a small peptide composed of three amino acids.
(251) The structure of chymotrypsin allows it to efficiently hydrolyze peptide bonds.
(252) The fluorophore was conjugated to a peptide to track its cellular localization.
(253) Proinsulin is cleaved by prohormone convertase 1 to form insulin and C-peptide.
(254) The rotamers of a peptide bond can affect the secondary structure of a protein.
(255) Exopeptidase is an enzyme that cleaves peptide bonds from the ends of proteins.
(256) The carboxyl group is essential for the formation of peptide bonds in proteins.
(257) Peptide synthesis is a complex process that requires precise chemical reactions.
(258) Peptide-based drugs have the advantage of being highly specific in their action.
(259) Peptide synthesis can be achieved through solid-phase or solution-phase methods.
(260) The array 'dipeptides' allows for the identification of novel peptide sequences.
(261) Pentapeptides can be synthesized using solid-phase peptide synthesis techniques.
(262) Solid-phase peptide synthesis enables the creation of complex peptide sequences.
(263) The amidin reagent was used to test for the presence of a specific peptide bond.
(264) Peptide-based biomaterials have shown promise in tissue engineering applications.
(265) Peptide fragments can be used to identify proteins in mass spectrometry analysis.
(266) The amphipathic peptide has both hydrophobic and hydrophilic amino acid residues.
(267) The array 'dipeptides' offers a valuable resource for studying peptide chemistry.
(268) The discovery of pentapeptides has revolutionized the field of peptide chemistry.
(269) The hydrolysates were analyzed for their peptide profile using mass spectrometry.
(270) Exopeptidase is highly specific in its recognition and cleavage of peptide bonds.
(271) The researcher used a preparative HPLC column to fractionate the peptide mixture.
(272) The octapeptide has been synthesized using advanced peptide chemistry techniques.
(273) The glycyl group can be easily protected or deprotected during peptide synthesis.
(274) Prolyl endopeptidase is an enzyme that cleaves peptide bonds at proline residues.
(275) Peptide conjugation allows for targeting and labeling in biomedical applications.
(276) The carbonyl group is a key feature in the formation of peptide bonds in proteins.
(277) The structure of endopeptidase allows it to access peptide bonds within a protein.
(278) The cecropin peptide is known for its ability to disrupt bacterial cell membranes.
(279) The enzyme acted enzymatically to cleave the peptide bond between two amino acids.
(280) The enzymatic hydrolysis of proteins yields peptones with varying peptide lengths.
(281) Angiotensin I is a peptide hormone that plays a role in regulating blood pressure.
(282) The neurotropic peptide was found to have a positive effect on cognitive function.
(283) The primary structure of a peptide refers to the linear arrangement of amino acids.
(284) The folding of a peptide into its native conformation is critical for its function.
(285) Tyrocidine is an antibiotic peptide produced by certain strains of Bacillus brevis.
(286) The body can synthesize dipeptides through a process called peptide bond formation.
(287) The carbamoyl group can be used as a linker in the synthesis of peptide conjugates.
(288) The linker peptide in the vaccine formulation helps to enhance the immune response.
(289) Peptide microarrays are used for high-throughput screening of peptide interactions.
(290) The cecropin peptide has been successfully used in the treatment of infected wounds.
(291) The peptide bond is responsible for the linear sequence of amino acids in a protein.
(292) Thrombin is a serine protease that cleaves specific peptide bonds in its substrates.
(293) Melanocyte-stimulating hormone is a peptide hormone produced by the pituitary gland.
(294) Peptide vaccines are being developed as a potential solution for infectious diseases.
(295) The amphipathic peptide has a hydrophilic region that interacts with water molecules.
(296) The amphipathic peptide has a hydrophobic region that interacts with membrane lipids.
(297) Angiotensin I is a precursor to angiotensin III, another biologically active peptide.
(298) Angiotensin I is a peptide hormone that is involved in the regulation of blood volume.
(299) The amphipathic peptide has a hydrophobic region that anchors it to the cell membrane.
(300) The peptide bond is formed between the alpha-amino group and the alpha-carboxyl group.
(301) The biuret method is based on the principle that peptide bonds react with copper ions.
(302) Aminopeptidase is an enzyme that cleaves amino acids from the N-terminus of a peptide.
(303) Alkylated derivatives of amino acids are important intermediates in peptide synthesis.
(304) The fluorophore was conjugated to a peptide for tracking protein-protein interactions.
(305) Glycyl is often used in peptide synthesis as a protective group for other amino acids.
(306) The conformational preferences of the peptide were determined through NMR spectroscopy.
(307) Researchers are studying the potential therapeutic applications of peptide-based drugs.
(308) The peptide bond is responsible for the unique three-dimensional structure of proteins.
(309) The function of carboxypeptidase is to remove the last amino acid from a peptide chain.
(310) The structure of carboxypeptidase allows it to bind to the carboxyl group of a peptide.
(311) Angiotensin I is a peptide hormone that is involved in the regulation of fluid balance.
(312) Kallikrein is a serine protease that cleaves specific peptide bonds in target proteins.
(313) The acylated form of the peptide was able to cross the blood-brain barrier more easily.
(314) Amides can be used as coupling agents in peptide synthesis to join amino acids together.
(315) Angiotensin is a peptide hormone that plays a crucial role in regulating blood pressure.
(316) The glycoprotein can be converted into a therapeutic peptide for targeted drug delivery.
(317) Thiol groups can be protected during peptide synthesis using specific protecting groups.
(318) Although kinin is a small peptide, it plays a crucial role in regulating blood pressure.
(319) The secretion of atrial natriuretic peptide helps to regulate fluid balance in the body.
(320) The peptide bond is essential for the function of enzymes and other biological molecules.
(321) Angiotensin I is a peptide hormone that plays a role in the regulation of blood pressure.
(322) The incretion of atrial natriuretic peptide helps regulate fluid and electrolyte balance.
(323) Aminopeptidase, which is a hydrolase enzyme, breaks the peptide bond between amino acids.
(324) The presence of carboxyl groups in amino acids allows for the formation of peptide bonds.
(325) The word pentapeptide refers to a specific type of peptide consisting of five amino acids.
(326) The cecropin peptide has been shown to inhibit the growth of multidrug-resistant bacteria.
(327) The peptide bond is highly rigid and restricts the conformational flexibility of proteins.
(328) Tyrocidine is a cyclic peptide that can be modified to enhance its antimicrobial activity.
(329) Angiotensin I is an inactive peptide that requires further processing to exert its effects.
(330) The quaternary structure of a peptide refers to its arrangement in a multi-subunit complex.
(331) The tripeptide sequence in this peptide hormone is responsible for its biological activity.
(332) The discovery of tyrocidine paved the way for the development of other peptide antibiotics.
(333) The biuret test is based on the reaction between copper ions and peptide bonds in proteins.
(334) The specificity of endopeptidases allows them to cleave specific peptide bonds in proteins.
(335) The conformational rearrangement of the peptide was induced by binding to a specific ligand.
(336) The primary function of rRNA is to catalyze peptide bond formation during protein synthesis.
(337) The endoenzyme, which is a type of protease, specifically targets peptide bonds in proteins.
(338) Kallikrein is involved in the formation of bradykinin, a peptide that promotes inflammation.
(339) The bibasic nature of the amino acid allows it to form peptide bonds with other amino acids.
(340) The peptide bond connects the carboxyl group of one amino acid to the amino group of another.
(341) Apply a peptide-infused moisturizer to protect from wrinkles and promote collagen production.
(342) Sulfhydryl groups can be protected during peptide synthesis using specific protecting groups.
(343) The study of pentapeptides has led to the development of new techniques for peptide synthesis.
(344) Aminopeptidase is responsible for removing amino acids from the N-terminus of a peptide chain.
(345) The biuret reaction involves the formation of a complex between copper ions and peptide bonds.
(346) Pentagastrin is a synthetic peptide that mimics the action of a natural hormone in the stomach.
(347) The amidin moiety can be easily incorporated into peptide sequences for drug delivery purposes.
(348) The production of pancreatic juice is influenced by the presence of gastric inhibitory peptide.
(349) Hirudin is a peptide that specifically inhibits thrombin, a key enzyme in blood clot formation.
(350) The peptide bond is formed between the carbonyl carbon and the nitrogen of adjacent amino acids.
(351) Trypsin cleaves peptide bonds specifically at the carboxyl side of lysine and arginine residues.
(352) The conformational flexibility of the peptide allows it to adopt different secondary structures.
(353) Aminopeptidase, which is an exopeptidase, removes amino acids one by one from the peptide chain.
(354) The cyanoethylated polystyrene was used as a support material for solid-phase peptide synthesis.
(355) The tertiary structure of a peptide is determined by interactions between amino acid side chains.
(356) Peptide-based antimicrobial agents are being explored as alternatives to traditional antibiotics.
(357) The divalency of the peptide bond allowed it to link two amino acids together in a protein chain.
(358) Carboxypeptidase is classified as an exopeptidase due to its action at the ends of peptide chains.
(359) Ribosomal RNA molecules are essential for the formation of peptide bonds during protein synthesis.
(360) The amphiphilic peptide was able to self-assemble into a stable structure in aqueous environments.
(361) Pentapeptides have been used as building blocks for the construction of larger peptide-based drugs.
(362) The peptide bond is formed through a nucleophilic attack of the amino group on the carbonyl carbon.
(363) Chymotrypsin has a preference for cleaving peptide bonds adjacent to large hydrophobic amino acids.
(364) The conformational transitions of the peptide were monitored using circular dichroism spectroscopy.
(365) The specificity of endopeptidase allows it to cleave peptide bonds at specific amino acid residues.
(366) Carboxypeptidase is an enzyme that cleaves amino acids from the carboxy terminus of a peptide chain.
(367) The chemical group known as the amide is responsible for the formation of peptide bonds in proteins.
(368) Angiotensin I is a precursor to angiotensin IV, a peptide with potential cognitive-enhancing effects.
(369) The proinsulin molecule contains a signal peptide that directs its transport to the secretory pathway.
(370) The conformational changes in the peptide backbone were crucial for its secondary structure formation.
(371) Amino acids contain both an amino group and a carboxyl group, which allows them to form peptide bonds.
(372) Growth hormone is a peptide hormone that stimulates growth and cell reproduction in humans and animals.
(373) The design of peptide-based therapeutics requires careful consideration of stability and bioavailability.
(374) The cecropin peptide has been shown to be effective against both Gram-positive and Gram-negative bacteria.
(375) Enterokinase is known for its ability to cleave the peptide bond between lysine and aspartic acid residues.
(376) The amino group is involved in the formation of peptide bonds between amino acids during protein synthesis.
(377) The cecropin peptide has been shown to have synergistic effects when combined with other antimicrobial agents.
(378) The amino acids in a peptide chain accrete with respect to peptide bond formation and side chain interactions.
(379) Aminopeptidase is an enzyme that catalyzes the hydrolysis of amino acids from the N-terminus of a peptide chain.
(380) Exopeptidase is an enzyme that catalyzes the hydrolysis of peptide bonds at the terminal amino acid residues of a protein.
(381) The denatured amino acids lost their three-dimensional structure, but they still formed peptide bonds, which linked them together.
(382) The carboxyl group is an important functional group in the structure of proteins, as it is involved in the formation of peptide bonds.
(383) Although the amino group is not directly involved in the formation of peptide bonds, it can influence the reactivity and stability of the adjacent carbonyl group through hydrogen bonding and electrostatic interactions.
Peptide meaning
Peptide is a term that refers to a short chain of amino acids that are linked together by peptide bonds. These chains can range in length from just a few amino acids to several hundred, and they play a crucial role in many biological processes. If you are looking to use the word peptide in a sentence, there are a few tips that can help you to do so effectively. Here are some suggestions:
1. Understand the context: Before you use the word peptide in a sentence, it is important to understand the context in which it is being used. Peptides can be found in a wide range of biological systems, from hormones and neurotransmitters to enzymes and structural proteins. Knowing the context can help you to choose the right words to use alongside peptide.
2. Use descriptive language: When using the word peptide in a sentence, it can be helpful to use descriptive language to help your reader understand what you are talking about.
For example, you might describe a peptide as "a short chain of amino acids" or "a building block of proteins."
3. Be precise: Peptides are a specific type of molecule, so it is important to be precise when using the word in a sentence. Avoid using vague or general terms like "chemical" or "compound" when referring to peptides, as this can make your writing less clear.
4. Use examples: If you are trying to explain the concept of peptides to someone who is unfamiliar with the term, it can be helpful to use examples to illustrate your point.
For example, you might explain that insulin is a peptide hormone that regulates blood sugar levels in the body.
5. Avoid jargon: While it is important to be precise when using the word peptide, it is also important to avoid using jargon or technical language that might be confusing to your reader. Try to use simple, straightforward language that is easy to understand.
Overall, using the word peptide in a sentence requires a good understanding of the term and its context, as well as the ability to communicate clearly and effectively. By following these tips, you can use the word peptide in a way that is both accurate and easy to understand.
The word usage examples above have been gathered from various sources to reflect current and historical usage of the word Peptide. They do not represent the opinions of TranslateEN.com.