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Server NetBIOS name or IP address for the computer, which may or may not be the same as its TCP/IP name. To translate this name into the address needed to reach the SMB host, Samba checks several places where the name may be assigned to an IP address. Samba checks the following (in the order shown) until it finds a match: the local /etc/hosts file, the local /etc/lmhosts file, a WINS server on the network, and responses to broadcasts on each local network interface to resolve the name. Share Name under which the printer is shared with the remote computer. It may be different from the name by which local users of the SMB printer know the printer. User Username is required by the SMB server system to give you access to the SMB printer. A username is not necessary if you are authenticating the printer based on sharelevel rather than user-level access control. With share-level access, you can add a password for each shared printer or file system. Password Password associated with the SMB username or the shared resource, depending on the kind of access control being used.

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ESI technology give some hope that inorganic salt-tolerant ionization sources can become a reality in the very near future In some cases nonvolatile buffers and salts can be removed on-line just prior to sample introduction into the ESI source (164) Alternatively, salt-tolerant modi cations of ESI can be considered Karas and co-workers noted that salt tolerance of nano-ESI is signi cantly higher than that of conventional ESI MS (165) This was attributed to the different initial droplet sizes (micrometer range for conventional ESI, and an order of magnitude smaller for nano-ESI) and higher surface charge density for nano-ESI generated droplets These two factors are expected to result in early ssion without extensive evaporation for the nano-ESI generated droplets, avoiding a dramatic increase in the salt concentration Indeed, the conventional ESI spectra closely resemble nano-ESI spectra acquired from solutions with about an order of magnitude higher salt concentration (165).

Another recently introduced modi cation of ESI, fused-droplet electrospray ionization (FD ESI) (166), also shows greater tolerance to inorganic salts and nonvolatile buffers Although the general appearance of FD ESI mass spectra of peptides and proteins is very close to those obtained with conventional ESI MS, the former show a very high salt tolerance FD ESI mass spectra of proteins could be obtained from solutions containing as much as 10% NaCl (ie, 17 M) or 25% (425 mM) NaH2 PO4 (425 mM) (166) 1142 Macromolecular Crowding Effect Modern biological MS in general, and ESI MS in particular, are very sensitive analytical techniques The superior sensitivity of ESI MS (compared to many other biophysical methods, such as NMR) is certainly a great advantage when only minute amounts of sample are available for the analyses.

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On the other hand, working with very concentrated samples can present a challenge for ESI MS (as well as MALDI MS) analysis Such situations are extremely rare, as the emphasis in most typical applications is placed on detecting analytes present at very low concentrations However, as MS is increasingly being looked at as a means of monitoring protein behavior under conditions that mimic the in vivo environment, such a limitation may become important This can be illustrated with our own attempts to monitor behavior (conformational dynamics and oligomerization) of hemoglobin under near-native conditions ESI mass spectra of bovine hemoglobin (Hb) in dilute solutions maintained at neutral pH and medium salt show signi cant tetramer dissociation, as expected from the general principles of chemical equilibria.

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However, our attempts to acquire Hb spectra using typical concentrations of this protein inside red blood cells (typical Hb concentration in red blood cells is 2 6 mM) have failed due to precipitous deterioration of the spectral quality once the protein concentration exceeds 100 M This dif culty can be ameliorated to a certain degree by using nano-ESI instead of conventional ESI The example considered above is quite unique, as the endogenous concentrations of most proteins are several orders of magnitude lower than that of.

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