Directions (Part I): Answer any 10 of the following 12 questions ...

Surajit

Description

• exposé

Page 1D:\paula\geology\gis\midterm.wpd Question 2 Ques. 1 Name:_______________________________ Directions (Part I): Answer any 10 of the following 12 questions. If you need more space, use the back of the paper. Each question in Part I is worth 6 points.

• wpd question
• michigan minnesota mississippi missouri montana nebraska nevada
• limitations of a grid data format
• data

Sujets

• Exposé
• Tennessee
• Messina
• Arizona
• Florida
• Missouri
• Montana
• Mississippi
• Minnesota
• Nebraska
• Nevada
• Míchigan

Informations

• Publié par: kepap
• Nombre de lectures: 111
• Langue: English

Extrait

Figure S1





















Figure S1: Secondary structures of Myr- M, Myr-P M and M. Far UV CD spectra of M (top
panel) in sodium phosphate buffer and Myr- M (middle panel) and Myr-P M (lower panel) in DPC
micelles.


Figure S2
Figure S2: M and P M in DPC micelles. Superposition of NOESY spectra , showing correlations
among the down field shifted aromatic & amide proton resonances ( 2 dimension) with upfield
shifted aliphatic resonance ( 1 dimension) of M (red contour) and Myr- M (black contour) in DPC
micelles (top panel) and P M (red contour) and Myr-P M (black contour) in DPC micelles (bottom
panel). A larger dispersion in chemical shift along the 2 dimension and more number of NOE
contacts can be seen for Myr- M and Myr-P M tails in DPC.


Figure S3




















Figure S3: Myr- M and Myr-P M in buffer solution. NOESY spectra, showing correlations
among the down field shifted aromatic & amide proton resonances ( 2 dimension) with upfield
shifted aliphatic resonance ( 1 dimension) of Myr- M (top panel) and Myr-P M (bottom panel) in
sodium phosphate buffer solutions.





Figure S4





















 
Figure S4: PRE of M and PM. Plot showing ratio of intensity of NH/C H correlations obtained
1 1from H- H two-dimensional NOESY spectra, in the absence (I ) and in the presence (I) of 1 mM 0
MnCl , of M and P M tail peptides in sodium phosphate buffer solution (bottom panel) and in 2
solution containing DPC micelles (top panel) as a function of residue.


Figure S5























Figure S5: Summary of sequential and medium range NOEs of M tail. Bar diagram showing
NOE connectivites for Myr- M (panel A), Myr-P M (panel B) and M (panel C).

Figure S6
























Figure S6: Sidechain-Sidechain NOEs of Myr- M and Myr-P M in DPC micelles. (A) NOE
connectivities among aromatic residues F5/Y9 for Myr- M (top panel) and Myr-P M (bottom panel).
(B) NOE connectivites among ring-protons of aromatic residues F5, Y9 with the aliphatic sidechain
proton resonances of residues L2, M12, M13 for Myr- M (left panel) and Myr-P M (right panel).

Figure S7



Figure S7: Interactions between tails of M and 2. Plot showing combined chemical shift changes
15 1 15of N and HN resonances of selected residues of N labeled M upon titration with unlabeled 2
15(top panel) and N labeled 2 upon titration with unlabeled synthetic M and P M tail peptides.



Figure S8






















Figure S8: FRET studies dansylated M (Dan- M) tail with 2 tail. (panel A) Fluorescence
emission spectra of Trp5 residue of non-myristoylated mutated 2 ( 2H5W, Table 1 in main text),
upon additions of Dan- M peptide in sodium phosphate buffer solution. (panel B) Fluorescence
emission spectra of Trp5 residue of non-myristoylated mutated 2 ( 2H5W, Table 1 in main text),
upon additions of phosphorylated dan- M peptide in sodium phosphate buffer solution. (panel C)
Fluorescence emission spectra of Trp 24 myristoylated 2 peptide in DPC micelles upon additions of
Dan- M peptide. 


Figure S9




Figure S9: Interactions between myristoylated 2 tail with dansylated M tails by FRET in
aqueous buffer solution. The emission spectra of Trp fluorescence of 2 tail upon the additions of
dansylated M (top panel) and dansylated phosphorylated M (bottom) in a mixture of sodium
phosphate buffer and acetonitrile.

Figure S10


Figure S10: Amino acid sequence comparison among representative  and  cytosolic tails of
integrins. Alignment of amino acid sequences of M tail (panel A) and 2 tail (panel B) with other
homologous integrins. All of the conserved amino acid residues are bold faced. The NPXY motifs in
 tails are underlined.