Adenosine triphosphate (ATP) binding cassette (ABC) transporters are transmembrane proteins which function to transport many substrates across membranes and ensure the fidelity of transcription and translation in an ATP dependent manner (Jones & George, 2004). These transporters can carry out their functions as there are information contained within molecular sequences that define their roles. Such information are usually in the form of motifs and are located at certain regions of their respective molecular sequences known as domains. These motifs are usually conserved (Bork & Koonin, 1996) and such an understanding becomes important in many areas of research. One of the research interests involves the development of novel treatments against the multi-drug resistant property of ABC transporters in treating relevant human diseases such as cystic fibrosis and Tangier disease (Stefková et al., 2004). With any of such novel applications, a substantial knowledge on sequence motifs in terms of their functional significance is required. In this essay, the discussion is limited to protein sequence signatures in nucleotide binding domains (NBDs) of ABC transporters relating to substrate translocation. It will be seen that the protein sequence motifs perform similar function across species, and any mutation can affect its overall function. However, it should also be noted that these motifs can result in slightly different mechanism in different species, and that they can perform their function at certain domains of the protein. The understanding of protein sequence signatures has to be first introduced before assessing their functional significance. Protein sequences are one dimensional string of amino acid letter codes that represent the ... ... middle of paper ... ...er B motif in the N-terminal nucleotide binding domain (NBD-1) of Cdr1p of Candida albicans has acquired a new role in ATP hydrolysis. Biochemistry, 45(49): 14726. Schmees, G., Stein, A., Hunke, S., Landmesser, H., & Schneider, E. (1999). Functional consequences of mutations in the conserved 'signature sequence' of the ATP-binding-cassette protein MalK. Eur J Biochem, 266(2): 420-430. Stefková, J., Poledne, R., & Hubácek, J. A. (2004). ATP-binding cassette (ABC) transporters in human metabolism and diseases. Physiological research / Academia Scientiarum Bohemoslovaca, 53(3): 235. Tanabe, K., Lamping, E., Nagi, M., Okawada, A., Holmes, A. R., Miyazaki, Y., Cannon, R. D., Monk, B. C., & Niimi, M. (2011). Chimeras of Candida albicans Cdr1p and Cdr2p reveal features of pleiotropic drug resistance transporter structure and function. Molecular microbiology, 82(2): 416-433.
The ATP is used for many cell functions including transport work moving substances across cell membranes. It is also used for mechanical work, supplying the energy needed for muscle contraction. It supplies energy not only to heart muscle (for blood circulation) and skeletal muscle (such as for gross body movement), but also to the chromosomes and flagella to enable them to carry out their many functions. A major role of ATP is in chemical work, supplying the needed energy to synthesize the multi-thousands of types of macromolecules that the cell needs to exist. ATP is also used as an on-off switch both to control chemical reactions and to send messages.
Dr. Akabas ended his paper with a summary of his results. He concluded that Gly-91, Lys-95, and Gln-98 all line the CFTR channel and are arranged in a helical formation. Dr. Akabas also talked about the problems and surprises he faced during his experiment, such as a missense mutation of Gly-91 to Arg. In the end, substituted-cysteine-accessibility method exceeded the expectations of many and contributed greatly to our knowledge of the CFTR channel. Even though more research and discovery is being done today, we will always remember Dr. Akabas’s experiment as being the basis of the CFTR science.
Hall, Linley Erin. “Understanding Genetics DNA and RNA.” New York: The Rosen Publishing Group, Inc., 2011. Print. 01 Apr. 2014.
Scientist have been researching cellular respiration “They discovered that when Stat 3 protein was missing, cells consumed less oxygen and produced less ATP, the key molecular form of cellular energy,” which means that the ene...
Humans, and all animals, use adenosine triphosphate (ATP) as the main energy source in cells. The authors of Biological Science 5th edition said that “In general, a cell contains only enough ATP [adenosine triphosphate] to last from 30 seconds to a few minutes”. It is that way “Because it has such high potential energy, ATP is unstable and is not stored”. They also state that “In an average second, a typical cell in your body uses an average of 10 million ATP molecules and synthesizes [makes] just as many”. In the human body trillions of cells exist. The average human body uses and makes 10,000,000,000,000,000 molecules of ATP every second. In one minute the human body uses 600,000,000,000,000,000 molecules of ATP. In one day the human body uses 864,000,000,000,000,000,000 molecules of ATP. In one year, this is equivalent to 365.25 days; the average human body uses and makes a huge amount, 315,576,000,000,000,000,000,000 molecules of ATP. For this example one mile is equal to one molecule of ATP. Light travels at approximately 186,000 mi/sec. It would take light roughly 53,763,440,860 years to travel that many miles. The sheer amount of ATP made in the cells of people is amazing! This essay will explain somewhat the main way of making all of those ATP molecules in aerobic organisms, aerobic cellular respiration. There are four steps that take place in aerobic cellular respiration, and they are: 1.Glycolysis; 2. Pyruvate Processing; 3. Citric Acid Cycle; 4. Electron Transport and Oxidative Phosphorylation (Allison, L. A. , Black, M. , Podgoroski, G. , Quillin, K. , Monroe, J. , Taylor E. 2014).
Proteogenomics is a kind of science field that includes proteomics and genomics. Proteomic consists of protein sequence information and genomic consists of genome sequence information. It is used to annotate whole genome and protein coding genes. Proteomic data provides genome analysis by showing genome annotation and using of peptides that is gained from expressed proteins and it can be used to correct coding regions.Identities of protein coding regions in terms of function and sequence is more important than nucleotide sequences because protein coding genes have more function in a cell than other nucleotide sequences. Genome annotation process includes all experimental and computational stages.These stages can be identification of a gene ,function and structure of a gene and coding region locations.To carry out these processes, ab initio gene prediction methods can be used to predict exon and splice sites. Annotation of protein coding genes is very time consuming process ,therefore gene prediction methods are used for genome annotations. Some web site programs provides these genome annotations such as NCBI and Ensembl. These tools shows sequenced genomes and gives more accurate gene annotations. However, these tools may not explain the presence of a protein. Main idea of proteogenomic methods is to identify peptides in samples by using these tools and also with the help of mass spectrometry.Mass spectrometry searches translation of genome sequences rather than protein database searching. This method also annotate protein protein interactions.MS/MS data searching against translation of genome can determine and identify peptide sequences.Thus genome data can be understood by using genomic and transcriptomic information with this proteogenomic methods and tools. Many of proteomic information can be achieved by gene prediction algorithms, cDNA sequences and comparative genomics. Large proteomic datasets can be gained by peptide mass spectrophotometry for proteogenomics because it uses proteomic data to annotate genome. If there is genome sequence data for an organism or closely related genomes are present,proteogenomic tools can be used. Gained proteogenomic data provides comparing of these data between many related species and shows homology relationships among many species proteins to make annotations with high accuracy.From these studies, proteogenomic data demonstrates frame shifts regions, gene start sites and exon and intron boundaries , alternative splicing sites and its detection , proteolytic sites that is found in proteins, prediction of genes and post translational modification sites for protein.
Simon, E. J., Reece, J. B., Dickey, J. L. (02/2012). Campbell Essential Biology with Physiology, 4th Edition [VitalSource Bookshelf version 6.2]. Retrieved from http://online.vitalsource.com/books/9781256902089
Mechanisms and Functions of ATP-Dependent Chromatin-Remodeling Enzymes Geeta J. Narlikar, Tom Owen-Hughes Email DOI: http://dx.doi.org/10.1016/j.cell.2013.07.011
"The Species of the Secondary Protein Structure. Virtual Chembook - Elmhurst College. Retrieved July 25, 2008, from http://www.cd http://www.elmhurst.edu/chm/vchembook/566secprotein.html Silk Road Foundation. n.d. - n.d. - n.d.
This turn of events presents us with an alarming problem. Strains of bacteria that are resistant to all prescribed antibiotics are beginning to appear. As a result, diseases such as tuberculosis and penicillin-resistant gonorrhea are reemerging on a worldwide scale (1). Resistance first appears in a population of bacteria through conditions that favor its selection. When an antibiotic attacks a group of bacteria, cells that are highly susceptible to the medicine will die.
Distinct characteristics are not only an end result of the DNA sequence but also of the cell’s internal system of expression orchestrated by different proteins and RNAs present at a given time. DNA encodes for many possible characteristics, but different types of RNA aided by specialized proteins sometimes with external signals express the needed genes. Control of gene expression is of vital importance for an eukaryote’s survival such as the ability of switching genes on/off in accordance with the changes in the environment (Campbell and Reece, 2008). Of a cell’s entire genome, only 15% will be expressed, and in multicellular organisms the genes active will vary according to their specialization. (Fletcher, Ivor & Winter, 2007).
9. These genes produce enzymes used in oxidative phosphorylation and provide instructions for making transfer RNA and ribosomal RNA.
This represents a large superfamily of enzymes encoded by CYP genes. They are hemoproteins with varying ...
A polypeptide chain is a series of amino acids that are joined by the peptide bonds. Each amino acid in a polypeptide chain is called a residue. It also has polarity because its ends are different. The backbone or main chain is the part of the polypeptide chain that is made up of a regularly repeating part and is rich with the potential for hydrogen-bonding. There is also a variable part, which comprises the distinct side chain. Each residue of the chain has a carbonyl group, which is good hydrogen-bond acceptor, and an NH group, which is a good hydrogen-bond donor. The groups interact with the functional groups of the side chains and each other to stabilize structures. Proteins are polypeptide chains that have 500 to 2,000 amino acid residues. Oligopeptides, or peptides, are made up of small numbers of amino acids. Each protein has a precisely defined, unique amino acid sequence, referred to as its primary structure. The amino acid sequences of proteins are determined by the nucleotide sequences of genes because nucleotides in DNA specify a complimentary sequence in RNA, which specifies the amino acid sequence. Amino acid sequences determine the 3D structures of proteins. An alteration in the amino acid sequence can produce disease and abnormal function. All of the different ways
"Within a single subunit [polypeptide chain], contiguous portions of the polypeptide chain frequently fold into compact, local semi-independent units called domains." - Richardson, 1981