alpha-Crystallin A Chain
alpha-Crystallin B Chain
Molecular Sequence Data
Amino Acid Sequence
Polymerase Chain Reaction
Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2 on chromosome 22q11.2. (1/70)PURPOSE: To identify the genetic defect for the Coppock-like cataract (CCL) affecting a Swiss family, which defect was unlinked to the chromosome 2q33-35 CCL locus. METHODS: A large family was characterized for linkage analysis by slit lamp examination or by the review of drawings made before cataract extraction. The affection status was attributed before genotyping, and the genotyping was masked to the affection status. Two-point and multipoint linkage analyses were performed using the MLINK and the LINKMAP components of the LINKAGE program package (ver. 5.1), respectively. Mutational analysis of candidate genes was performed by a combination of direct cycle sequencing and an amplification refractory mutation system assay. RESULTS: Ten individuals were affected with the CCL phenotype. The disease was autosomal dominant and appeared to be fully penetrant. A new CCL locus was identified on chromosome 22q11.2 within a 11.67-cM interval (maximum lod score [Zmax] = 4.14; theta = 0). Mutational analysis of the CRYBB2 candidate gene identified a disease-causing mutation in exon 6. This sequence change was identical with that previously described to be associated with the cerulean cataract, a clinically distinct entity. CONCLUSIONS: The CCL phenotype is genetically heterogeneous with a second gene on chromosome 22q11.2, CRYBB2. The CCL and the cerulean cataract are two distinct clinical entities associated with the same genetic defect. This work provides evidence for a modifier factor that influences cataract formation and that remains to be identified. (+info)
Expression of betaB(2)-crystallin mRNA and protein in retina, brain, and testis. (2/70)PURPOSE: To evaluate the expression of betaB(2)-crystallin mRNA and protein in rat, bovine, and human nonlens and nonocular tissues. METHODS: betaB(2)-crystallin mRNA levels were detected by RT-PCR. betaB(2)-crystallin protein was purified from rat and bovine tissues by FPLC chromatography. FPLC fractions were analyzed by immunoblotting. The identity of betaB(2)-crystallin protein, isolated from the retina, was confirmed by protein microsequencing. RESULTS: betaB(2)-crystallin transcript was detected in rat brain, rat testis, and human retina by RT-PCR. betaB(2)-crystallin transcript was not found in rat lung, heart, ovary, spleen, thymus, kidney, and liver or in human brain and testis. betaB(2)-crystallin protein was partially purified from and its identity confirmed in rat brain, rat testis, and bovine retina. The bovine retinal protein was further confirmed to be authentic betaB(2)-crystallin by protein microsequencing. CONCLUSIONS: These results establish that betaB(2)-crystallin mRNA and protein are expressed in tissues outside of the lens and outside of the eye including retina, brain, and testis. Extralenticular and extraocular expression of betaB(2)-crystallin, coupled with its participation in phosphorylation pathways, suggests that it has nonrefractive functions in these tissues. (+info)
Aey2, a new mutation in the betaB2-crystallin-encoding gene of the mouse. (3/70)PURPOSE: During an ethylnitrosourea (ENU) mutagenesis screen, mice were tested for the occurrence of dominant cataracts. One particular mutant was found that caused progressive opacity and was referred to as Aey2. The purpose of the study was to provide a morphologic description, to map the mutant gene, and to characterize the underlying molecular lesion. METHODS: Isolated lenses were photographed, and histologic sections of the eye were analyzed according to standard procedures. Linkage analysis was performed using a set of microsatellite markers covering all autosomal chromosomes. cDNA from candidate genes was amplified after reverse transcription of lens mRNA. RESULTS: The cortical opacification visible at eye opening progressed to an anterior suture cataract and reached its final phenotype as total opacity at 8 weeks of age. There was no obvious difference between heterozygous and homozygous mutants. The mutation was mapped to chromosome 5 proximal to the marker D5Mit138 (8.7 +/- 4.2 centimorgan [cM]) and distal to D5Mit15 (12.8 +/- 5.4 cM). No recombinations were observed to the markers D5Mit10 and D5Mit25. This position makes the genes within the betaA4/betaB-crystallin gene cluster excellent candidate genes. Sequence analysis revealed a mutation of T-->A at position 553 in the Crybb2 gene, leading to an exchange of Val for GLU: It affects the same region of the Crybb2 gene as in the Philly mouse. Correspondingly, the loss of the fourth Greek key motif is to be expected. CONCLUSIONS: The Aey2 mutant represents the second allele of Crybb2 in mice. Because an increasing number of beta- and gamma-crystallin mutations have been reported, a detailed phenotype-genotype correlation will allow a clearer functional understanding of beta- and gamma-crystallins. (+info)
Identification and properties of anti-chaperone-like peptides derived from oxidized bovine lens betaL-crystallins. (4/70)Thermal aggregation of betaL-crystallin was higher in the presence of peptide fragments generated from oxidized and trypsin-digested betaL-crystallin compared with thermal aggregation of the control proteins without oxidized betaL-crystallin fragments. Increased aggregation of betaL-crystallin was also observed despite the presence of alpha-crystallin (which has anti-aggregating properties) in the system. Self-aggregation of the oxidized betaL-crystallin fragments per se was not observed under the experimental conditions. Reverse-phase HPLC analysis of the precipitate obtained after heating a mixture of betaL-crystallin and oxidized betaL-crystallin fragments revealed that more than one peptide co-precipitates with betaL-crystallin. Electrospray mass spectrometry analysis of the peptides revealed that the molecular weight(s) of the peptides ranged from 1400-1800. Tandem mass spectrometry and a data base search revealed that two of the peptides originated from betaA4-crystallin (LTIFEQENFLGR, residues 121-132) and betaB3-crystallin (AINGTWVGYEFPGYR, residues 153-167) respectively. Oxidized synthetic peptides representing the same sequence were also found to enhance the aggregation of betaL-crystallin in a manner similar to oxidized lens betaL-crystallin peptides. These data suggest that the polypeptides generated after oxidation and proteolysis of betaL-crystallins interact with denaturing proteins and facilitate their aggregation and light scattering, thus behaving like anti-chaperones. (+info)
Decreased heat stability and increased chaperone requirement of modified human betaB1-crystallins. (5/70)PURPOSE: To determine how deamidation and partial loss of the N- and C-terminal extensions alter the heat stability of betaB1-crystallin. METHODS: Human lens betaB1, a deamidated betaB1, Q204E, and alphaA-crystallins were expressed. Truncated betaB1 was generated by proteolytic removal of part of its terminal extensions. The aggregation and precipitation of these proteins due to heating was monitored by circular dichroism and light scattering. The effect of heat on the stability of both monomers and oligomers was investigated. The flexibility of the extensions in wild type and deamidated betaB1 was assessed by 1H NMR spectroscopy. RESULTS: With heat, deamidated betaB1 precipitated more readily than wild type betaB1. Similar effects were obtained for either monomers or oligomers. Flexibility of the N-terminal extension in deamidated betaB1 was significantly reduced compared to the wild type protein. Truncation of the extensions further increased the rate of heat-induced precipitation of deamidated betaB1. The presence of the molecular chaperone, alphaA-crystallin, prevented precipitation of modified betaB1s. More alphaA was needed to chaperone the truncated and deamidated betaB1 than deamidated betaB1 or truncated betaB1. CONCLUSIONS: Deamidation and truncation of betaB1 led to destabilization of the protein and decreased stability to heat. Decreased stability of lens crystallins may contribute to their insolubilization and cataract formation. (+info)
A nonsense mutation in CRYBB1 associated with autosomal dominant cataract linked to human chromosome 22q. (6/70)Autosomal dominant cataract is a clinically and genetically heterogeneous lens disorder that usually presents as a sight-threatening trait in childhood. Here we have mapped dominant pulverulent cataract to the beta-crystallin gene cluster on chromosome 22q11.2. Suggestive evidence of linkage was detected at markers D22S1167 (LOD score [Z] 2.09 at recombination fraction [theta] 0) and D22S1154 (Z=1.39 at theta=0), which closely flank the genes for betaB1-crystallin (CRYBB1) and betaA4-crystallin (CRYBA4). Sequencing failed to detect any nucleotide changes in CRYBA4; however, a G-->T transversion in exon 6 of CRYBB1 was found to cosegregate with cataract in the family. This single-nucleotide change was predicted to introduce a translation stop codon at glycine 220 (G220X). Expression of recombinant human betaB1-crystallin in bacteria showed that the truncated G220X mutant was significantly less soluble than wild type. This study has identified the first CRYBB1 mutation associated with autosomal dominant cataract in humans. (+info)
BetaB1-crystallin: identification of a candidate ciliary body uveitis antigen. (7/70)PURPOSE: Perineuclear anti-neutrophil cytoplasmic antibody (pANCA), a marker antibody present in 12% of patients with anterior uveitis, recognizes cytoplasmic antigens in the nonpigmented ciliary body epithelium, a probable site of immunologic reactivity in this inflammatory disease. In this study, a recombinantly isolated pANCA monoclonal antibody was used to identify the corresponding antigenic target(s) in the ciliary body. METHODS: Proteins from microdissected eye bank ocular ciliary body tissue were used to identify the corresponding ANCA antigen. Parallel two-dimensional protein gels were used for simultaneous identification of candidate antigenic protein spots by Western blot analysis and as a source of material for proteomic analysis. Multiple independent methods including Western blot analysis, confocal microscopy, and RT-PCR were used to provide additional characterization of the candidate protein. RESULTS: Proteomic analysis suggested that beta B1 (betaB1)-crystallin is the primary ciliary body antigen. The presence of betaB1-crystallin in the human ciliary body was confirmed by Western blot with a betaB1 specific anti-peptide antibody. Confocal microscopy revealed colocalization of the antigenic reactivity of both anti-betaB1 antibody and monoclonal pANCA. RT-PCR confirmed the presence of betaB1-crystallin RNA in the ciliary body tissues. CONCLUSIONS: This study identified betaB1-crystallin as a new cytoplasmic ciliary body antigenic target of a marker autoantibody associated with uveitis. This characterization of betaB1-crystallin outside the lens raises questions about its extralenticular expression, intracellular role, and potential target of inflammation in uveitis. (+info)
Improving the performance of DomainParser for structural domain partition using neural network. (8/70)Structural domains are considered as the basic units of protein folding, evolution, function and design. Automatic decomposition of protein structures into structural domains, though after many years of investigation, remains a challenging and unsolved problem. Manual inspection still plays a key role in domain decomposition of a protein structure. We have previously developed a computer program, DomainParser, using network flow algorithms. The algorithm partitions a protein structure into domains accurately when the number of domains to be partitioned is known. However the performance drops when this number is unclear (the overall performance is 74.5% over a set of 1317 protein chains). Through utilization of various types of structural information including hydrophobic moment profile, we have developed an effective method for assessing the most probable number of domains a structure may have. The core of this method is a neural network, which is trained to discriminate correctly partitioned domains from incorrectly partitioned domains. When compared with the manual decomposition results given in the SCOP database, our new algorithm achieves higher decomposition accuracy (81.9%) on the same data set. (+info)
Progesterone congeners are synthetic derivatives of the hormone progesterone that are used in various medical applications. These compounds are similar in structure to progesterone and have similar biological effects, but they may have different pharmacological properties and side effects. Progesterone congeners are used in a variety of medical settings, including: 1. Hormonal contraception: Some progesterone congeners are used in combination with estrogen to prevent pregnancy. These contraceptives are taken orally, as a patch, or as an injection. 2. Menopause treatment: Progesterone congeners are sometimes used to treat symptoms of menopause, such as hot flashes and vaginal dryness. 3. Endometriosis treatment: Progesterone congeners may be used to treat endometriosis, a condition in which tissue similar to the lining of the uterus grows outside the uterus. 4. Infertility treatment: Some progesterone congeners are used to support pregnancy in women who are having difficulty conceiving. 5. Gynecological disorders: Progesterone congeners may be used to treat gynecological disorders such as uterine fibroids and abnormal uterine bleeding. It is important to note that the use of progesterone congeners may have side effects, and they may not be suitable for everyone. It is important to discuss the potential risks and benefits of these medications with a healthcare provider before starting treatment.
Crystallins are a group of proteins that are found in the lens of the eye. They are responsible for maintaining the transparency and shape of the lens, which is essential for focusing light onto the retina and allowing us to see clearly. There are several different types of crystallins, including alpha, beta, and gamma crystallins, each with its own unique structure and function. In the medical field, crystallins are often studied in the context of age-related eye diseases such as cataracts, which are caused by the accumulation of abnormal protein aggregates in the lens.
Beta-crystallin B chain is a protein that is a component of the eye lens. It is one of the five major types of beta-crystallins, which are small, heat-stable proteins that help to maintain the shape and transparency of the lens. Beta-crystallin B chain is encoded by the CRYBB4 gene and is synthesized in the lens epithelial cells. It is thought to play a role in the formation and maintenance of the lens fibers, which are responsible for the focusing of light in the eye. Mutations in the CRYBB4 gene can lead to lens abnormalities and cataracts, a clouding of the lens that can cause vision loss.
Beta-crystallin A chain is a protein that is a component of the eye lens. It is one of the major structural proteins in the lens and plays a role in maintaining the shape and transparency of the lens. Beta-crystallin A chain is encoded by the CRYBA1 gene. Mutations in this gene can lead to cataracts, a clouding of the lens that can cause vision loss.
Gamma-crystallins are a group of proteins that are found in the lens of the eye. They are the most abundant proteins in the lens and play a crucial role in maintaining the transparency and shape of the lens. Gamma-crystallins are also involved in regulating the concentration of ions and other molecules in the lens, which helps to maintain the proper osmotic balance and prevent the lens from swelling or shrinking. Mutations in the genes that encode gamma-crystallins can lead to a variety of eye disorders, including cataracts and other lens abnormalities.
Beta-crystallins are a family of proteins that are primarily found in the lens of the eye. They are responsible for maintaining the transparency and shape of the lens, which is essential for clear vision. There are several different types of beta-crystallins, each with its own unique function and location within the lens. Beta-crystallins are also found in other tissues, including the retina, cornea, and skin. In these tissues, they may play a role in maintaining tissue structure and function. Mutations in the genes that encode beta-crystallins can lead to a variety of eye disorders, including cataracts, a condition in which the lens becomes cloudy and impairs vision. Other disorders associated with beta-crystallin mutations include congenital cataracts, juvenile cataracts, and some forms of retinal dystrophy.
Ricin is a highly toxic protein produced by the castor bean plant (Ricinus communis). It is classified as a plant toxin and is considered one of the most potent toxins known to man. In the medical field, ricin is primarily studied as a potential bioterrorism agent due to its ease of production and high toxicity. It is also used in research to study the mechanisms of protein toxicity and as a tool for developing new treatments for various diseases. However, ricin is not currently used in any licensed medical treatments or vaccines. Ingestion or inhalation of ricin can cause severe respiratory and gastrointestinal symptoms, and exposure to high levels of ricin can be fatal. Therefore, it is important to handle ricin with extreme caution and to follow proper safety protocols when working with this substance.
Alpha-crystallin A chain is a protein that is encoded by theCRYAA gene in humans. It is a member of the alpha-crystallin family of proteins, which are found in the lens of the eye and play a role in maintaining the transparency and shape of the lens. Alpha-crystallin A chain is a small, heat-stable protein that is composed of two alpha-crystallin A subunits and two alpha-crystallin B subunits. It is thought to play a role in protecting the lens from damage caused by oxidative stress and other environmental factors. Mutations in the CRYAA gene can lead to a group of eye disorders known as cataracts, which are characterized by the clouding of the lens and can cause vision loss.
Alpha-crystallins are a group of small, heat-stable proteins that are found in the lens of the eye. They are also present in other tissues, such as the retina and the cornea. Alpha-crystallins are important for maintaining the transparency and structure of the lens, and they play a role in protecting the lens from damage caused by oxidative stress and other factors. In addition, alpha-crystallins have been shown to have anti-inflammatory and anti-aging properties, and they may play a role in the development of age-related eye diseases, such as cataracts and age-related macular degeneration.
Alpha-crystallin B chain is a protein that is encoded by theCRYAB gene in humans. It is a component of the alpha-crystallin family of proteins, which are found in the lens of the eye and play a role in maintaining the transparency and shape of the lens. The alpha-crystallin B chain is a small, heat-stable protein that is thought to help stabilize the alpha-crystallin complex and protect it from denaturation. Mutations in the CRYAB gene have been associated with several eye disorders, including cataracts and glaucoma.
Delta-crystallins are a group of proteins that are found in the lens of the eye. They are one of the major types of crystallins, which are the proteins that make up the transparent lens of the eye. Delta-crystallins are responsible for maintaining the shape and transparency of the lens, and they are also involved in regulating the flow of water and ions into and out of the lens. Delta-crystallins are synthesized by the cells of the lens, called lens epithelial cells, and they are secreted into the lens by these cells. They are small, globular proteins that are composed of about 200 amino acids, and they have a molecular weight of approximately 25,000 daltons. There are several different types of delta-crystallins, which are classified based on their amino acid sequence and their location within the lens. These include alpha-delta crystallins, beta-delta crystallins, and gamma-delta crystallins. Each type of delta-crystallin has a slightly different function within the lens, and they work together to help maintain the structure and function of the lens. Abnormalities in the production or function of delta-crystallins can lead to a variety of eye problems, including cataracts, which are a clouding of the lens that can cause vision loss. Cataracts are a common age-related eye condition, but they can also be caused by other factors, such as injury, disease, or exposure to certain medications or environmental toxins.
A cataract is a clouding of the natural lens in the eye that affects vision. The lens is responsible for focusing light onto the retina, which is the light-sensitive tissue at the back of the eye. When the lens becomes cloudy, it can interfere with the ability of light to pass through and be focused properly, leading to vision problems. Cataracts are a common age-related condition, but they can also be caused by injury, disease, or certain medications. Symptoms of cataracts may include blurry vision, difficulty seeing at night, sensitivity to light, double vision, and the appearance of halos around lights. Treatment for cataracts typically involves surgery to remove the cloudy lens and replace it with an artificial lens. This procedure, called cataract surgery, is generally safe and effective, and can significantly improve vision in people with cataracts.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
Abrin is a potent toxin found in the seeds of the Abrus precatorius plant, also known as the rosary pea. It is a type of lectin, which is a type of protein that binds to specific carbohydrates on the surface of cells. In the medical field, abrin is primarily used as a research tool to study the effects of toxins on cells and organisms. It has also been used in the development of antitumor drugs and as a potential treatment for certain types of cancer. However, abrin is also a dangerous poison that can cause serious harm if ingested or inhaled. Symptoms of abrin poisoning can include nausea, vomiting, abdominal pain, diarrhea, difficulty breathing, and even death. Treatment for abrin poisoning typically involves supportive care, such as fluid replacement and oxygen therapy, as well as medications to manage symptoms and prevent complications.
In the medical field, "Bungarus" refers to a genus of venomous snakes found in Asia, including the common Indian krait (Bungarus caeruleus) and the Chinese krait (Bungarus multicinctus). These snakes are known for their potent neurotoxic venom, which can cause paralysis and respiratory failure if left untreated. Envenomation by Bungarus snakes is a medical emergency and requires prompt medical attention, including antivenom therapy.
Interleukin-1beta (IL-1β) is a type of cytokine, which is a signaling molecule that plays a crucial role in the immune system. It is produced by various types of immune cells, including macrophages, monocytes, and dendritic cells, in response to infection, injury, or inflammation. IL-1β is involved in the regulation of immune responses, including the activation of T cells, B cells, and natural killer cells. It also promotes the production of other cytokines and chemokines, which help to recruit immune cells to the site of infection or injury. In addition to its role in the immune system, IL-1β has been implicated in a variety of inflammatory and autoimmune diseases, including rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. It is also involved in the pathogenesis of certain types of cancer, such as breast cancer and ovarian cancer. Overall, IL-1β is a key mediator of inflammation and immune responses, and its dysregulation has been linked to a range of diseases and conditions.
In the medical field, a base sequence refers to the specific order of nucleotides (adenine, thymine, cytosine, and guanine) that make up the genetic material (DNA or RNA) of an organism. The base sequence determines the genetic information encoded within the DNA molecule and ultimately determines the traits and characteristics of an individual. The base sequence can be analyzed using various techniques, such as DNA sequencing, to identify genetic variations or mutations that may be associated with certain diseases or conditions.
Beta 2-Microglobulin (β2M) is a small protein that is produced by most cells in the body, including immune cells such as T cells and B cells. It is a component of the major histocompatibility complex (MHC) class I molecules, which are found on the surface of most cells and are responsible for presenting antigens (foreign substances) to the immune system. In the medical field, β2M is often used as a marker of kidney function. High levels of β2M in the blood can indicate kidney damage or failure, as the kidneys are responsible for removing β2M from the bloodstream. In addition, high levels of β2M have been associated with an increased risk of certain types of cancer, including multiple myeloma and prostate cancer. β2M is also used as a diagnostic tool in the laboratory to help identify and monitor certain diseases and conditions, such as multiple myeloma, autoimmune disorders, and viral infections. It is also used as a component of some types of cancer treatments, such as immunotherapy.
List of MeSH codes (D12.776)
List of A1 genes, proteins or receptors
Protease inhibitor (biology)
List of MeSH codes (D08)
Protein S (Myxococcus xanthus)
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- crystallin zeta [Source:HGNC Symbol;Ac. (gsea-msigdb.org)
- Serum and plasma beta 2 microglobulin values have emerged as markers for the activation of the cellular immune system, as well as a tumor marker in certain hematologic malignancies. (medscape.com)
- Low serum levels of beta 2 microglobulin essentially indicate decreased disease activity in conditions for which beta 2 microglobulin is used as a prognostic marker ( multiple myeloma , lymphoma, leukemia ) or the absence of such a disease process. (medscape.com)
- Increased serum beta 2 microglobulin levels reflect increased activity of the disease process in question and can be an exquisitely sensitive marker for this purpose in many hematologic disorders. (medscape.com)
- In such cases, serum beta 2 microglobulin levels are usually normal, since the dysfunction is in tubular reabsorption. (medscape.com)
- Beta 2 microglobulin can be determined in urine, serum, or plasma samples. (medscape.com)
- This light-protein chain, which can be shed into serum, is called beta 2 microglobulin. (medscape.com)
- Serum beta 2 microglobulin has now been identified as an important prognostic marker in a large number of hematologic and nonhematologic disorders. (medscape.com)
- Beta 2 microglobulin is an 11.8-kD protein (see first image below), which forms one of the chains of the major histocompatibility complex (MHC) class I molecule normally present on the surface of every nucleated cell in the human body. (medscape.com)
- It begins when glucose molecules attach themselves to proteins, initiating a chain of chemical reactions that result in protein crosslinking. (thinmdmedspa.com)
- In vitro, the synthesis and release of beta 2 microglobulin can be induced by acidosis, endotoxin, or inflammatory cytokines. (medscape.com)
- Up to 25% of pediatric cataract cases are inherited, with half of the known mutant genes belonging to the crystallin family. (bvsalud.org)
- These antigens have a heavy chain and an associated light chain. (medscape.com)
- Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical. (cipsm.de)
- Carnosine, a dipeptide composed of beta-alanine and 1-histidine, has shown remarkable potential in combating glycation and its detrimental effects on the aging process. (thinmdmedspa.com)
- The acidic subunit of beta-crystallins. (bvsalud.org)
- A subclass of ANTIFREEZE PROTEINS that are globular, 6.5 kDa in size and contain compact beta-sheet structures. (lookformedical.com)
- Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. (nih.gov)
- This light-protein chain, which can be shed into serum, is called beta2 microglobulin. (medscape.com)
- Beta2 microglobulin is an 11.8-kD protein (see first image below), which forms one of the chains of the major histocompatibility complex (MHC) class I molecule normally present on the surface of every nucleated cell in the human body. (medscape.com)
- Protein S from Myxococcus xanthus is a member of the beta gamma-crystallin superfamily. (protabank.org)
- Vicky then went to Berlin to join the group of Prof Hartmut Oschkinat during which time she switched from some initial solution NMR work to solid-state protein NMR, working predominantly on the large beta-barrel porin, OmpG. (bris.ac.uk)
- Most of the molecular machines built by cells are composed of protein and nucleic acid chains. (rcsb.org)
- The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. (lookformedical.com)
- Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. (nih.gov)
- crystallin gamma N [Source. (gsea-msigdb.org)
- PARP1 Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 354 amino acids (662-1014a.a.) and having a molecular mass of 39.6 kDa. (kendallscientific.com)
- PARP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (233-583a.a) and having a molecular mass of 42.5kDa. (kendallscientific.com)
- POLL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300) and having a molecular mass of 36.0 kDa.POLL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. (kendallscientific.com)
- Description: NAP1L4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375) and having a molecular mass of 45.2 kDa. (hiv-pharmacogenomics.org)
- The order of amino acids as they occur in a polypeptide chain. (lookformedical.com)
- ferritin light chain [Sour. (gsea-msigdb.org)
- Atomic structures have revealed how these chains are built and how they fold into functional molecular machines. (rcsb.org)