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- Models of higher-order compaction suggest that thenucleosomal fiber is _____ into a shorter but widerfiber.I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?Imagine you need to move a large protein from one region in the cell to another. Which of the following proteins would be able to do this? Onuclease O myoglobin O kinesin Oligase O hemoglobin O myosin
- Define Dynamic instability depends on the presenceor absence of a GTP-β-tubulin cap.Woite Short 2otes oo +RNA.It is not an easy matter to assign particular func-tions to specific components of the basal lamina, sincethe overall structure is a complicated composite materialwith both mechanical and signaling properties. Nidogen,for example, cross-links two central components of thebasal lamina by binding to the laminin γ-1 chain and totype IV collagen. Given such a key role, it was surprisingthat mice with a homozygous knockout of the gene fornidogen-1 were entirely healthy, with no abnormal phe-notype. Similarly, mice homozygous for a knockout of thegene for nidogen-2 also appeared completely normal. Bycontrast, mice that were homozygous for a defined muta-tion in the gene for laminin γ-1, which eliminated just thebinding site for nidogen, died at birth with severe defectsin lung and kidney formation. The mutant portion of thelaminin γ-1 chain is thought to have no other functionthan to bind nidogen, and does not affect laminin struc-ture or its ability to assemble into the basal lamina.…
- coded for oxyte Based on your pases would h oxytocin?The steps involved in the T→ R transition in when oxygen binds to hemoglobin are outlined below. Place them in the correct order (1 = first thing to happen), assuming that it is the oxygen-binding that initiates the transition and that the process occurs in discrete steps. The proximal histidine is pulled by the heme iron. The F helix is pulled out of place, breaking a network of salt bridges. The iron is pulled into the plane of the protoporphyrin IX ring. Oxygen binds to the heme. < <= A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [F] = ab M
- you have isolated a new protein called STICKY. you can predict from comparisons with other known proteins that STICKY contains bHLH domain. Predict the function of STICKY and rationale forthe importnce of these domains in sticky function.The movements of single motor-protein moleculescan be analyzed directly. Using polarized laser light, it ispossible to create interference patterns that exert a cen-trally directed force, ranging from zero at the center to afew piconewtons at the periphery (about 200 nm from thecenter). Individual molecules that enter the interferencepattern are rapidly pushed to the center, allowing them tobe captured and moved at the experimenter’s discretion.Using such “optical tweezers,” single kinesin mol-ecules can be positioned on a microtubule that is fixed toa coverslip. Although a single kinesin molecule cannotbe seen optically, it can be tagged with a silica bead andtracked indirectly by following the bead (Figure Q16–3A).In the absence of ATP, the kinesin molecule remains at thecenter of the interference pattern, but with ATP it movestoward the plus end of the microtubule. As kinesin movesalong the microtubule, it encounters the force of the inter-ference pattern, which simulates the load…Identify a protein that can contain a temperature-sensitive mutation that would explain these observations O Atvtoptesme protein that is unabte to bind to IMP aarc OAlgn unction protein tut hindh tightly to IMP 3C Acelt corte protein that unuble tu bind to IMP37C OAtnnsmemtrrane proten that binds tighely to Mat 37C O An entracelr matrie pootein that bt tightly 1o İMPat 37C