1887

Color Plates

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • HTML
    6.50 Kb
  • XML
    8.00 Kb
Add to My Favorites
You must be logged in to use this functionality
Loading full text...

Full text loading...

/deliver/fulltext/10.1128/9781555815813/cp01.html?itemId=/content/book/10.1128/9781555815813.cp01&mimeType=html&fmt=ahah

Figures

Image of Color Plate 1 (Chapter 6).

Click to view

Color Plate 1 (Chapter 6).

Stereo diagram depicting superimposition of highly homologous cold-shock proteins from (red, PDB entry: 1C9O chain A, BcCSP) and (green, PDB entry: 1CSP, BsCSP). The backbones of the two proteins are shown as thin lines and the nonconserved residues between the two protein structures are shown as balls and sticks (see text for details). For the sake of clarity, the conserved residues between the two proteins are not shown. The N- and C-termini are indicated by the first (Met 1) and the last residues (Leu 66) in BcCSP. Arg 3, which along with Leu 66 mostly confers thermostability on BcCSP (Perl et al., 2000), is also shown. Cold-shock proteins have emerged as a model system to understand molecular factors involved in protein thermostability. Modulation of protein electrostatics appears to be responsible for the greater stability of BcCSP. However, this is not achieved by incorporation of additional salt bridges or ion pairs in BcCSP. In this sense, the case of the cold-shock proteins appears exceptional.

Citation: Gerday C, Glansdorff N. 2007. Color Plates, In Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Color Plate 2 (Chapter 19).

Click to view

Color Plate 2 (Chapter 19).

Crystallographic structures of halophilic proteins. PYMOL was used to represent the electrostatic potential at the surface of the proteins. The names of halophilic proteins are defined in Table 1. LDH, the lactate dehydrogenase from the nonhalophilic , is shown for comparison. TBP is the TATA-binding box protein from the hyperthermophile .

Citation: Gerday C, Glansdorff N. 2007. Color Plates, In Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Color Plate 3 (Chapter 19).

Click to view

Color Plate 3 (Chapter 19).

Crystallographic structures of R207S, R292S mutant of MalDH. Two orthogonal views are presented, with the four polypeptide chains of the tetramer shown in ribbons of different colours; NADH is shown in a stick representation, chloride ions as grey balls, and water as small red dots.

Citation: Gerday C, Glansdorff N. 2007. Color Plates, In Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Color Plate 4 (Chapter 20).

Click to view

Color Plate 4 (Chapter 20).

Macroscopic growths of acidophilic microbial communities at two mine sites in north Wales: (a) stalactite-like (“pipe”) growths and (b) surface slimes within a disused pyrite mine and (c) streamer growths in acid waters draining an abandoned copper mine.

Citation: Gerday C, Glansdorff N. 2007. Color Plates, In Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error