From chemistry-request@server.ccl.net Fri Aug 27 09:16:07 1999 Received: from ns.apbiotech.com (ns.apbiotech.com [192.36.117.130]) by server.ccl.net (8.8.7/8.8.7) with ESMTP id JAA10662 for ; Fri, 27 Aug 1999 09:16:06 -0400 From: enrique.carredano@eu.apbiotech.com Received: from mailgate.se.apbiotech.com (unverified [193.235.253.52]) by ns.apbiotech.com (Rockliffe SMTPRA 3.3.1) with ESMTP id for ; Fri, 27 Aug 1999 15:10:40 +0200 Received: from eunotes.apbiotech.com (unverified [193.180.20.124]) by mailgate.se.apbiotech.com (Rockliffe SMTPRA 3.3.1) with SMTP id for ; Fri, 27 Aug 1999 15:06:24 +0200 Received: by eunotes.apbiotech.com(Lotus SMTP MTA v4.6.3 (778.2 1-4-1999)) id 412567DA.004D7DCB ; Fri, 27 Aug 1999 15:06:24 +0100 X-Lotus-FromDomain: XYNET To: chemistry@ccl.net Message-ID: <412567DA.004D7AB4.00@eunotes.apbiotech.com> Date: Fri, 27 Aug 1999 15:07:34 +0100 Subject: CCL:effects of temperature on hydrophobicity Mime-Version: 1.0 Content-type: text/plain; charset=us-ascii Content-Disposition: inline Does any one know something about the effects of temperature (say, an increase >from 20 to 40 degrees C) on the hydrophobicity properties of a protein? Best regards Enrique Enrique Carredano, MSc, PhD +46 (0)18 16 50 00 tel Polymer and Surface Chemistry +46 (0)18 16 50 42 direct Amersham Pharmacia Biotech +46 (0)18 16 63 96 fax Bjorkg 30, 751 84 Uppsala Sweden enrique.carredano@eu.apbiotech.com From chemistry-request@server.ccl.net Fri Aug 27 10:04:11 1999 Received: from mailrelay2.lrz-muenchen.de (mailrelay2.lrz-muenchen.de [129.187.254.102]) by server.ccl.net (8.8.7/8.8.7) with ESMTP id KAA10890 for ; Fri, 27 Aug 1999 10:04:06 -0400 Received: from ruppert.phys.chemie.tu-muenchen.de by mailrelay2.lrz-muenchen.de for @dfvgate.lrz-muenchen.de:chemistry@server.ccl.net; Fri, 27 Aug 1999 15:57:25 +0200 Received: from physik.tu-muenchen.de by ruppert.phys.chemie.tu-muenchen.de via ESMTP (940816.SGI.8.6.9/930416.SGI) for id PAA17159; Fri, 27 Aug 1999 15:57:23 +0200 Sender: tmehnert@physik.tu-muenchen.de Message-Id: <37C69942.34938B6C@physik.tu-muenchen.de> Date: Fri, 27 Aug 1999 15:57:22 +0200 From: Mehnert Thomas X-Mailer: Mozilla 4.04 [en] (X11; I; IRIX 5.3 IP22) MIME-Version: 1.0 To: chemistry@server.ccl.net Subject: TINKER Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Hi alltogether Does anybody know how to define the charge of one molecule within a two molecule cluster system by using the TINKER program? Thanks in advance Th. Mehnert From chemistry-request@server.ccl.net Sat Aug 28 13:29:10 1999 Received: from news.mtu.edu (root@news.mtu.edu [141.219.70.11]) by server.ccl.net (8.8.7/8.8.7) with ESMTP id NAA17608 for ; Sat, 28 Aug 1999 13:29:10 -0400 Received: from mtu.edu (root@mtu.edu [141.219.70.1]) by news.mtu.edu (8.8.8/8.8.8) with ESMTP id NAA03865; Sat, 28 Aug 1999 13:22:24 -0400 (EDT) Received: from phy.mtu.edu (phy.mtu.edu [141.219.151.64]) by mtu.edu (8.8.8/8.8.8) with ESMTP id NAA19477; Sat, 28 Aug 1999 13:22:23 -0400 (EDT) Received: from localhost (anil@localhost) by phy.mtu.edu (8.8.8/8.8.7/mtumailer-1.2) with ESMTP id NAA02881; Sat, 28 Aug 1999 13:22:22 -0400 (EDT) X-Authentication-Warning: phy.mtu.edu: anil owned process doing -bs Date: Sat, 28 Aug 1999 13:22:22 -0400 (EDT) From: "Anil K. Kandalam" To: enrique.carredano@eu.apbiotech.com cc: chemistry@ccl.net Subject: Re: CCL:effects of temperature on hydrophobicity In-Reply-To: <412567DA.004D7AB4.00@eunotes.apbiotech.com> Message-ID: MIME-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII > Does any one know something about the effects of temperature (say, an increase > >from > 20 to 40 degrees C) on the hydrophobicity properties of a protein? > Enrique > ######## Enrique, With an increase in temperature in the range of 20-40C, there is change in the confirmational folding of the amino rather an imino acid PROLINE which would maintain the protein stable, with an increased stability of the protein as a function of its hydrophobic microenvironment in all those proteins where proline happens to be an essential component of the protein. In those proteins which do not have the iminoacid proline as a component, the activity regulation of the protein as a function of temperature where activation of the active sites of the protein is far more greater in comparison to deactivation. In general, majority of the proteins after their synthesis, fold in a cooperative fashion which demands the natural physiological conditions as it involves nothing but the interaction of aminoacids. Hence the temperature increase within the physiological range would facilitate easy folding by the increased interactions between the activated hydrophobic aminoacids. ANIL KUMAR KANDALAM ------------------------------------------------------------------------------- Address: | off: Dept. of Physics, | res: 612 Garnet Street, apt.#4, 1400 Townsend Drive, | HOUGHTON,MI-49931, Michigan Tech. Univ., | USA. HOUGHTON, MI-49931. | USA | Ph: (906) 487 2591 | Ph: (906) 482 0885 e-mail: anil@mtu.edu URL: http://www.phy.mtu.edu/~anil -------------------------------------------------------------------------------